heme has been researched along with tryptophan in 271 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 87 (32.10) | 18.7374 |
| 1990's | 36 (13.28) | 18.2507 |
| 2000's | 78 (28.78) | 29.6817 |
| 2010's | 58 (21.40) | 24.3611 |
| 2020's | 12 (4.43) | 2.80 |
| Authors | Studies |
|---|---|
| Tsong, TY | 1 |
| Roberts, J; Rosenfeld, HJ | 1 |
| Badawy, AA | 3 |
| Hrkal, Z; Kodícĕk, M; Suttnar, J; Vodrázka, Z | 1 |
| Brady, FO | 1 |
| Keller, RM; Wüthrich, K | 1 |
| Erecińska, M; Vanderkool, JM | 1 |
| Badawy, AA; Evans, M | 3 |
| Bucci, E; Gryczynski, Z; Tenenholz, T | 1 |
| Davidson, MG; Goodin, DB; Mauk, AG; Roe, JA; Smith, M | 1 |
| Davies, AM; Greenwood, C; Guillemette, JG; Mauk, AG; Moore, GR; Smith, M; Thurgood, AG | 1 |
| Gafni, A; Mersol, JV; Steel, DG | 1 |
| Alpert, B; Ridgeway, JM; Szabo, AG; Willis, KJ; Zuker, M | 1 |
| Bradley, D; Campagnoni, AT; Morris, SJ; Stoner, GL | 1 |
| Correia, MA; Lunetta, JM | 1 |
| Erman, JE; Kraut, J; Mauro, JM; Vitello, LB | 1 |
| Myers, D; Palmer, G | 1 |
| Hitchcock, MJ; Katz, E | 1 |
| Pandya, KP; Rao, GS; Siddiqui, SM | 1 |
| Alvarado, A; Bonkovsky, HL; Lincoln, BC; Setty, N | 1 |
| Correia, MA; Litman, DA; Lunetta, JM | 1 |
| Henry, ER; Hochstrasser, RM | 1 |
| Dalvit, C; Wright, PE | 1 |
| Radding, JA | 1 |
| Pogson, CI; Salter, M | 1 |
| Correia, MA; Litman, DA | 2 |
| Kleinfeld, AM; Lukacovic, MF | 1 |
| Dickerson, RE | 1 |
| Winfield, ME | 1 |
| Feigelson, P; Koike, K | 2 |
| Fontana, A; Toniolo, C; Vita, C | 1 |
| Brady, FO; Feigelson, P; Rajagopalan, KV | 1 |
| Cohen, JS; Fisher, WR; Schechter, AN | 1 |
| Pettigrew, GW | 1 |
| Groudinsky, O; Keller, R; Wüthrich, K | 1 |
| Feigelson, P; Schutz, G | 1 |
| Brady, FO; Feigelson, P; Forman, HJ; Monaco, ME; Schutz, G | 1 |
| Seifert, J | 1 |
| Ho, C; Ladner, JE; Perutz, MF; Simon, SR | 1 |
| Morgan, WT; Muller-Eberhard, U | 1 |
| Perutz, MF | 1 |
| Williamson, AR | 1 |
| Schimke, RT | 1 |
| Baillie, DL; Chovnick, A | 1 |
| Feigelson, P; Forman, HJ | 1 |
| Coulson, AF; Yonetani, T | 1 |
| Huntley, TE; Strittmatter, P | 1 |
| Folin, M; Galiazzo, G; Gennari, G; Jori, G | 1 |
| Billups, C; Horwitz, J; Kay, E; Shannon, LM; Strickland, EH; Wilchek, M | 1 |
| McKellar, JR; Weightman, JA; Williams, RJ | 1 |
| Hayaishi, O | 1 |
| Satoh, T | 1 |
| Allis, JW; Steinhardt, J | 1 |
| Hayaishi, O; Ishimura, Y; Nozaki, M | 1 |
| Anderson, SR; Brunori, M; Weber, G | 1 |
| McGowan, EB; Stellwagen, E | 1 |
| Risler, JL | 1 |
| Craigie, JS; Laycock, MV | 1 |
| Feigelson, P; Maeno, H | 1 |
| Nanzyo, N; Sano, S | 1 |
| Horwitz, J; Kay, E; Shannon, LM; Strickland, EH | 1 |
| Fouts, JR; Magus, RD | 1 |
| Madras, BK; Missala, K; Sourkes, TL | 1 |
| Herskovits, TT | 1 |
| Johnson, BP; Li, TK | 1 |
| Galiazzo, G; Jori, G; Scoffone, E | 1 |
| Feigelson, P; Hayaishi, O; Ishimura, Y | 2 |
| Knox, WE; Piras, MM; Tokuyama, K | 1 |
| Baudras, A; Di Franco, A; Iwatsubo, M; Labeyrie, F | 1 |
| Hayaishi, O; Yamamoto, S | 1 |
| Stellwagen, E; Van Rooyan, S | 1 |
| Dawson, JH; Sono, M | 1 |
| Bersohn, R; Mitra, S | 1 |
| Krogmann, DW; Markley, JL; Ulrich, EL | 1 |
| Hochstrasser, RM; Negus, DK | 1 |
| Burk, RF; Correia, MA | 1 |
| Brunet, JE; Gonzalez, GA; Sotomayor, CP | 1 |
| Buterbaugh, GG; Sadler, EM; Weiner, M | 1 |
| Gerrard, JM; Peterson, DA; Rao, GH; White, JG | 1 |
| Badawy, AA; Morgan, CJ | 1 |
| Badawy, AA; Morgan, CJ; Welch, AN | 1 |
| Beychok, S; Craik, CS; Vallette, I; Waks, M | 1 |
| Alpert, B; Fontaine, MP; Jameson, DM | 1 |
| Eads, JC; Jordan, T; Spiro, TG | 1 |
| Iwamoto, Y; Kido, R; Lee, IS; Tsubaki, M | 2 |
| Das, TK; Mazumdar, S | 1 |
| Coggins, JR; Kelly, SM; Lindsay, JG; Malarkey, K; McKnight, J; Miles, JS; Munro, AW; Price, NC; Thomson, AJ | 1 |
| Banci, L; Bertini, I; Ferrer, JC; Mauk, AG; Morris, IK; Smith, KM; Smith, M; Turano, P | 1 |
| Bucci, E; Fronticelli, C; Gryczynski, Z; Tenenholz, T | 1 |
| Durham, B; Geren, L; Hahm, S; Kraut, J; Miller, MA; Millett, F | 1 |
| Baudry, P; Callebert, J; Deybach, JC; Nordmann, Y; Puy, H; Touitou, Y | 1 |
| Goodin, DB; McRee, DE | 1 |
| Barnard, ML; Diep, D; Gurdian, S; Ladd, M; Turrens, JF | 1 |
| Abraham, NG; Bock, G; Fuchs, D; Kappas, A; Levere, RD; Lutton, JD; Wachter, H; Weiss, G; Werner-Felmayer, G | 1 |
| Baumgartner, M; Bogdan, A; Callebert, J; Deybach, JC; Nordmann, Y; Puy, H; Touitou, Y; Voisin, P | 1 |
| Brodersen, DE; Chen, Z; Davidson, VL; Durley, RC; Mathews, FS; Merli, A; Morini, B; Rossi, GL | 1 |
| Haiech, J; Leclerc L'Hostis, E; Leclerc, L; Marden, MC; Poyart, C | 1 |
| Durham, B; Geren, L; Mei, H; Miller, MA; Millett, F; Pielak, GJ; Saunders, A; Waldner, JL; Wang, K; Wang, X | 1 |
| Chan, CK; Eaton, WA; Hofrichter, J; Hu, Y; Rousseau, DL; Takahashi, S | 1 |
| Khan, KK; Mazumdar, S; Mitra, S; Modi, S; Roberts, GC; Sutcliffe, M | 1 |
| Chiu, F; McDonald, MJ; Morris, A; Vasudevan, G | 1 |
| Wittung-Stafshede, P | 1 |
| Beck, DL; Goldman, BS; Kranz, RG; Monika, EM | 1 |
| Almo, SC; Ho, C; Ho, NT; Puius, YA; Zou, M | 1 |
| Kery, V; Kraus, JP; Poneleit, L | 1 |
| Constans, AJ; Lecomte, JT; Mayer, MR; Sukits, SF | 1 |
| Bucci, E; Gryczynski, Z | 1 |
| Aust, SD; Nie, G; Reading, NS; Timofeevski, SL | 1 |
| Atkins, WM; Daggett, V; Storch, EM | 1 |
| Keppler, BK; Kozłowski, H; Trynda-Lemiesz, L | 1 |
| Rousseau, DL; Yeh, SR | 1 |
| Kitagawa, T; Nagai, M; Nagatomo, S; Tsuneshige, A; Yonetani, T | 1 |
| Hendrich, MP; Ho, C; Ho, NT; Jeong, ST | 1 |
| Chattopadhyay, K; Mazumdar, S | 1 |
| Ahmad, F; Ahmad, R; Sinha, A; Yadav, S | 1 |
| Behr, J; Hellwig, P; Mäntele, W; Michel, H | 1 |
| Eaton, WA; Hagen, SJ | 1 |
| Guidry, J; Moczygemba, C; Wittung-Stafshede, P | 1 |
| Adak, S; Stuehr, DJ; Wang, Q | 1 |
| David, PS; Dutt, PS; Hill, BC; Jia, Z; Wathen, B | 1 |
| Hillar, A; Loboda, A; Loewen, PC; Mauk, AG; Pauls, R; Peters, B; Zhang, H | 1 |
| Bendall, DS; Carrell, CJ; Cramer, WA; Howe, CJ; Ponamarev, MV; Schlarb, BG; Smith, JL | 1 |
| Daff, S; Sagami, I; Sato, Y; Shimizu, T | 1 |
| Döpner, S; Harris, TR; Hildebrand, DP; Hildebrandt, P; Mauk, AG; Rosell, FI | 1 |
| Iizuka, T; Mukai, M; Nakamura, H; Nakamura, K; Shiro, Y | 1 |
| Daff, S; Sagami, I; Shimizu, T; Yumoto, T | 1 |
| Blodig, W; Doyle, WA; Piontek, K; Smith, AT | 1 |
| Argyris, EG; Paterson, Y; Vanderkooi, JM | 1 |
| Farid, RS; Xu, Z | 1 |
| Adak, S; Stuehr, DJ | 1 |
| Furtmüller, PG; Jakopitsch, C; Loewen, PC; Obinger, C; Regelsberger, G; Rueker, F; Switala, J | 1 |
| Blodig, W; Piontek, K; Smith, AT | 1 |
| Adak, S; Couture, M; Rousseau, DL; Stuehr, DJ | 1 |
| Hara, I; Itoh, S; Lee, K; Ueno, T; Ueyama, N; Watanabe, Y | 1 |
| Rafferty, SP; Wilson, DJ | 1 |
| Adachi, O; Devreese, B; Duine, JA; Hacisalihoglu, A; Iwabuki, H; Jongejan, JA; Kim, JK; Kuroda, S; Okajima, T; Tanizawa, K; Van Beeumen, J; Vandenberghe, I | 1 |
| Ghosh, S; Hemann, C; Hille, R; Meade, AL; Stuehr, DJ; Wang, ZQ; Wei, CC | 1 |
| Aoyagi, M; Arvai, AS; Getzoff, ED; Ghosh, S; Stuehr, DJ; Tainer, JA | 1 |
| Behere, DV; Kamal, JK | 1 |
| Counts Gerber, N; Kosarikov, DN; Lee, JM; Uversky, VN | 1 |
| Ahuja, U; Ren, Q; Thöny-Meyer, L | 1 |
| Heering, HA; Smith, AT; Smulevich, G | 1 |
| Haruta, N; Kitagawa, T; Mizutani, Y | 1 |
| Dreyfuss, BW; Gabilly, ST; Hamel, PP; Merchant, S; Xie, Z | 1 |
| Bowler, BE; Smith, CR; Wandschneider, E | 1 |
| Adak, S; Dawson, JH; Goodin, DB; Ikeda-Saito, M; Perera, R; Pond, AE; Sono, M; Stuehr, DJ; Tomita, T; Voegtle, HL | 1 |
| Bhaskar, B; Farmer, PJ; Immoos, CE; Poulos, TL; Shimizu, H; Sulc, F | 1 |
| Littlejohn, TK; Takikawa, O; Truscott, RJ; Walker, MJ | 1 |
| Davidson, VL; Graichen, ME; Liu, A; Pearson, AR; Wang, Y; Wilmot, CM | 1 |
| GREENGARD, O | 1 |
| KOIKE, K; OKUI, S | 2 |
| KNOX, WE; OGATA, M | 1 |
| Ahuja, U; Thöny-Meyer, L | 1 |
| Auer, M; Ivancich, A; Jakopitsch, C; Obinger, C; Un, S | 1 |
| Bigotti, MG; Brunori, M; Cutruzzolà, F; Musto, R; Travaglini-Allocatelli, C | 1 |
| Chen, Z; Ost, TW; Schelvis, JP | 1 |
| Célier, C; Grosclaude, J; Marden, MC; Pato, C; Rezaei, H | 1 |
| Proshlyakov, DA | 1 |
| Balakrishnan, G; Case, MA; Ho, C; McLendon, GL; Pevsner, A; Spiro, TG; Tsai, CH; Wu, Q | 1 |
| Bertrand, T; Brown, KA; Eady, NA; Jamart-Grégoire, B; Jones, JN; Nagy, JM; Raven, EL | 1 |
| Austin, CJ; Jamie, JF; Kosim-Satyaputra, P; Matin, A; Mizdrak, J; Parker, MW; Polekhina, G; Roberts, TH; Sirijovski, N; Truscott, RJ; Willows, RD | 1 |
| Rousseau, DL; Yeh, SR; Zhong, S | 1 |
| Olson, JS; Phillips, GN; Zhang, W | 1 |
| Banci, L; Barker, PD; Bruix, M; Ciofi-Baffoni, S; de Lumley Woodyear, T; Fersht, AR; Garcia, P; Johnson, CM; Ramachandra Shastry, MC; Rico, M; Roder, H | 1 |
| Adachi, S; Hara, I; Lu, Y; Makino, Y; Ohki, T; Pfister, TD; Ueno, T; Ueyama, N; Watanabe, Y | 1 |
| Panda, K; Santolini, J; Stuehr, DJ; Wang, Q; Wang, ZQ; Wei, CC | 1 |
| Ghiladi, RA; Knudsen, GM; Medzihradszky, KF; Ortiz de Montellano, PR | 1 |
| Giovannelli, JL; Ho, C; Ho, NT; Lukin, JA; Simplaceanu, V; Wiltrout, ME | 1 |
| Heck, DE; Laskin, DL; Laskin, JD; Mariano, TM; Mishin, V; Vetrano, AM | 1 |
| Crespo, A; Estrin, DA; Fernández, ML; Martí, MA | 1 |
| Barra, AL; Böttger, LH; Contzen, J; Galander, M; Jung, C; Lendzian, F; Richter, M; Schünemann, V; Trautwein, AX | 1 |
| Mizutani, Y; Sato, A | 1 |
| Davidson, VL; Feng, M; Li, X; Tachikawa, H; Wang, Y | 1 |
| Aono, S; Inagaki, S; Kitagawa, T; Kubo, M; Mizutani, Y; Uchida, T; Yoshioka, S | 1 |
| Samelson-Jones, BJ; Yeh, SR | 1 |
| Bale, S; Begley, TP; Crane, BR; Ealick, SE; Kang, SA; Mukherjee, T; Zhang, Y | 1 |
| Badyal, SK; Bottrill, AR; Metcalfe, CM; Mistry, SC; Pipirou, Z; Raven, EL; Rawlings, BJ | 1 |
| Heath, MD; Poole, RK; Shepherd, M | 1 |
| Kitajima, S; Kurioka, M; Shimaoka, T; Yokota, A | 1 |
| Takusagawa, F; Yamada, T | 1 |
| de Vries, S; Ludwig, B; Richter, OM; Wiertz, FG | 1 |
| Bolognesi, M; Couture, M; Guertin, M; LaBarre, M; Milani, M; Ouellet, H | 1 |
| Basran, J; Bottrill, AR; Cooper, CE; Efimov, I; Mistry, SC; Pipirou, Z; Raven, EL; Svistunenko, DA | 1 |
| Basova, LV; Bayir, H; Belikova, NA; Jiang, J; Kagan, VE; Kapralov, AA; Kurnikov, IV; Tyurin, VA; Tyurina, YY; Vladimirov, YA; Vlasova, II; Zhao, Q | 1 |
| Davydov, R; García-Serres, R; Hoffman, BM; Huynh, BH; Kim, SH; Lippard, SJ; McCormick, MS; Murray, LJ; Naik, SG | 1 |
| Basova, LV; Bychkova, VE; Kutyshenko, VP; Mauk, AG; Tiktopulo, EI | 1 |
| Davidson, VL; Fu, R; Krebs, C; Lee, S; Li, X; Liu, A | 1 |
| Guo, L; Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D | 1 |
| Basran, J; Bottrill, AR; Guallar, V; Metcalfe, CL; Mistry, SC; Murphy, EJ; Pipirou, Z; Raven, EL | 1 |
| Basran, J; Chapman, SK; Chauhan, N; Eaton, G; Efimov, I; Jenkins, PR; Lee, M; Mowat, CG; Rafice, SA; Raven, EL; Thackray, SJ | 1 |
| Couture, M; Driscoll, D; Gélinas, S; Lang, J; Rafferty, SP | 1 |
| Barros, MP; Bechara, EJ; Dyszy, FH; Faria, PA; Mano, CM; Nantes, IL; Nascimento, OR; Prieto, T | 1 |
| Bellezza, F; Cipiciani, A; Latterini, L; Posati, T; Sassi, P | 1 |
| Lu, C; Nickel, E; Nienhaus, GU; Nienhaus, K; Yeh, SR | 1 |
| Kao, YT; Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D | 1 |
| Naismith, JH; van Pée, KH; Zhu, X | 1 |
| Abu Tarboush, N; Davidson, VL; Shin, S | 1 |
| Ogura, T; Shiro, Y; Sugimoto, H; Yanagisawa, S | 1 |
| Davidson, VL; Goblirsch, BR; Wilmot, CM; Yukl, ET | 1 |
| Bundschuh, FA; Hannappel, A; Ludwig, B | 1 |
| Arroyo Mañez, P; Boechi, L; Estrin, DA; Lu, C; Luque, FJ; Martí, MA; Poole, RK; Shepherd, M; Wilson, JL; Yeh, SR | 1 |
| De Cristofaro, R; Lancellotti, S; Novarese, L | 1 |
| Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D | 1 |
| Bräm, O; Cannizzo, A; Chergui, M; Consani, C | 1 |
| Kittikool, D; Sibmooh, N; Srihirun, S; Tangnitipong, S; Thaptimthong, T; Udomsangpetch, R; Unchern, S | 1 |
| Basran, J; Chapman, SK; Chauhan, N; Efimov, I; Mowat, CG; Raven, EL; Sun, X | 1 |
| Davidson, VL; Feng, M; Jensen, LM; Liu, A; Wei, X; Wilmot, CM; Yukl, ET | 1 |
| Davidson, VL; Liu, A | 1 |
| Basran, J; Efimov, I; Handa, S; Millett, ES; Mowat, CG; Raven, EL | 1 |
| Bauer, CE; Dragnea, V; Yin, L | 1 |
| Barry, SM; Challis, GL | 1 |
| Martínez, ÁT; Martínez, MJ; Mate, MJ; Morales, M; Romero, A; Ruiz-Dueñas, FJ | 1 |
| Wilmot, CM; Yukl, ET | 1 |
| Abu Tarboush, N; Davidson, VL; Geng, J; Liu, A; Shin, S | 1 |
| Blanc, B; DuBois, JL; Lukat-Rodgers, GS; Rodgers, KR | 1 |
| Chao, WC; Chou, PT; Chou, SC; Lu, JF; Pan, TA; Wang, JS; Wang, LH; Yang, HC | 1 |
| Auböck, G; Chergui, M; Consani, C; van Mourik, F | 1 |
| Iram, A; Naeem, A | 1 |
| Winkler, JR | 1 |
| Davidson, VL; Dornevil, K; Geng, J; Liu, A | 1 |
| Davidson, VL; Wilmot, CM | 1 |
| Abu Tarboush, N; Davidson, VL; Feng, M; Shin, S; Wilmot, CM; Yukl, ET | 1 |
| Davidson, VL; Shin, S | 1 |
| Goodwin, DC; Ndontsa, EN; Njuma, OJ | 1 |
| Geng, J; Liu, A | 1 |
| Didik, J; Domazou, AS; Gebicka, L; Gebicki, JL; Koppenol, WH; van der Meijden, B | 1 |
| Bielecki, M; Olczak, T; Wójtowicz, H | 1 |
| Donald, LJ; Hosseinzadeh, P; Ivancich, A; Karaduman, N; Loewen, PC; Lu, Y; Miner, KD; Pfister, TD | 1 |
| Galisteo, J; Herraiz, T | 1 |
| Ding, W; Gu, J; Liu, ZJ; Meng, B; Ouyang, S; Wu, D | 1 |
| Du, KJ; Lin, YW; Nie, CM; Shu, XG; Wen, GB | 1 |
| Choi, EY; Kang, MJ; Lee, C; Lee, HB; Lee, J; Lee, YK; Min, CK; Noh, S; Shin, DM; Yi, EC | 1 |
| Divsalar, A; Ghalandari, B; Harifi, AR; Moradi, M; Saboury, AA | 1 |
| Davis, I; Geng, J; Liu, A | 1 |
| Choi, M; Davidson, VL; Feng, M; Li, C; Shin, S; Williamson, HR; Wilmot, CM | 1 |
| Al Haddad, A; Auböck, G; Chergui, M; Monni, R; van Mourik, F | 1 |
| Hori, H; Iizuka, T; Ishimura, Y; Makino, R; Mashima, K; Obayashi, E; Shiro, Y | 1 |
| Jarzęcki, AA; Kruft, BI; Magliozzo, RS | 1 |
| Boulet, L; Faure, P; Flore, P; Le Gouellec, A; Pépin, JL; Toussaint, B | 1 |
| Arnold, FH; Cahn, JK; Dodani, SC; Kiss, G; Pande, VS; Su, Y | 1 |
| Malkowski, MG; Orlando, BJ | 1 |
| Yuasa, HJ | 1 |
| Besley, NA; Hirst, JD; Suess, CJ | 1 |
| Davidson, VL; Ma, Z | 1 |
| Ener, ME; Gray, HB; Winkler, JR | 1 |
| Fita, I; Rovira, C; Wang, B | 1 |
| Davidson, VL | 1 |
| Dokainish, H; Kitao, A; Mizuno, M; Mizutani, Y; Tran, DP; Yamashita, S | 1 |
| Gray, HB; Winkler, JR | 1 |
| Chen, C; Chen, J; Guo, C; Luo, S; Tong, L; Tong, Y; Xiang, S; Xu, K | 1 |
| Hara, M; Kayama, K; Ogura, T; Shiro, Y; Sugimoto, H; Yanagisawa, S | 1 |
| Estrin, DA; Issoglio, F; Pedron, FN; Scherlis, DA | 1 |
| Biswas, P; Dai, Y; Stuehr, DJ | 1 |
| Kim, JS; Murarka, VC; Poulos, TL | 1 |
| Kitao, A; Mizuno, M; Mizutani, Y; Takemura, K; Yamashita, S | 1 |
| Britt, RD; Chakarawet, K; Dwaraknath, S; Ledray, AP; Lu, Y; Merchen, C; Rao, G; Sponholtz, MR; Van Stappen, C | 1 |
| Gray, HB; Ravanfar, R; Sheng, Y; Winkler, JR | 1 |
| Liu, J; Offei, SD; Scott, EE; Yoshimoto, FK | 1 |
| Arrell, CA; Bacellar, C; Biednov, M; Bressler, C; Cannelli, O; Chergui, M; Cirelli, C; Gawelda, W; Ingle, RA; Johnson, PJM; Khakhulin, D; Kinschel, D; Knopp, G; Kubicek, K; Lima, FA; Mancini, GF; Menzi, S; Milne, CJ; Ozerov, D; Pamfilidis, G; Rodriguez-Fernandez, A; Rouxel, JR; Szlachetko, J; Zhao, Y | 1 |
| Biswas, P; Stuehr, DJ | 1 |
| Du, YL; Li, H; Li, W; Shi, X; Wu, M; Zhao, G; Zhao, Z | 1 |
| Anashkina, AA; Kaluzhny, DN; Kuleshova, ID; Makarov, AA; Maksimov, GV; Mitkevich, VA; Parshina, EY; Petrushanko, IY; Poluektov, YM; Zaripov, PI | 1 |
17 review(s) available for heme and tryptophan
| Article | Year |
|---|---|
The functions and regulation of tryptophan pyrrolase.
Topics: Allosteric Regulation; Aminolevulinic Acid; Animals; Dactinomycin; Feedback; Gluconeogenesis; Heme; Kinetics; Kynurenine; Liver; NAD; NADP; Rats; Tryptophan; Tryptophan Oxygenase | 1977 |
Tryptophan 2,3-dioxygenase: a review of the roles of the heme and copper cofactors in catalysis.
Topics: Adrenocorticotropic Hormone; Animals; Binding, Competitive; Copper; Electron Spin Resonance Spectroscopy; Heme; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kinetics; Lasers; Liver; Protein Binding; Protein Conformation; Pseudomonas; Rats; Spectrophotometry; Spectrophotometry, Infrared; Spectrophotometry, Ultraviolet; Tryptophan; Tryptophan Oxygenase | 1975 |
Structure and function of hemoglobin.
Topics: Amino Acid Sequence; Heme; Hemoglobins; Models, Chemical; Tryptophan; Tyrosine | 1969 |
The biosynthesis of multichain proteins.
Topics: Alkaline Phosphatase; Antibody Formation; Chymotrypsin; Escherichia coli; Genetic Code; Genotype; Globins; Heme; Hemoglobins; Hydro-Lyases; Insulin; Molecular Biology; Mutation; Phenotype; Protein Biosynthesis; RNA, Messenger; Tryptophan; Zinc | 1969 |
Lignin peroxidase structure and function.
Topics: Fungi; Heme; Hydroxylation; Lignin; Models, Molecular; Oxidation-Reduction; Peroxidases; Plants; Protein Conformation; Recombinant Proteins; Structure-Activity Relationship; Tryptophan | 2001 |
UV optical absorption by protein radicals in cytochrome c oxidase.
Topics: Animals; Carbon Monoxide; Cattle; Copper; Electron Transport Complex IV; Free Radicals; Heme; Hydrogen-Ion Concentration; In Vitro Techniques; Myocardium; Oxygen; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 2004 |
Biochemical properties of indoleamine 2,3-dioxygenase: from structure to optimized design of inhibitors.
Topics: Animals; Crystallography, X-Ray; Enzyme Inhibitors; Gene Expression; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kynurenine; Models, Molecular; Protein Conformation; Tryptophan | 2011 |
Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.
Topics: Bacterial Proteins; Biocatalysis; Coenzymes; Free Radicals; Heme; Indolequinones; Iron-Sulfur Proteins; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan | 2012 |
Heme-containing dioxygenases involved in tryptophan oxidation.
Topics: Biocatalysis; Dioxygenases; Heme; Humans; Oxidation-Reduction; Substrate Specificity; Tryptophan | 2012 |
Tailoring reactions catalyzed by heme-dependent enzymes: spectroscopic characterization of the L-tryptophan-nitrating cytochrome P450 TxtE.
Topics: Amino Acid Sequence; Biocatalysis; Cytochrome P-450 Enzyme System; Escherichia coli; Gene Expression; Heme; Indoles; Iron; Isoenzymes; Molecular Sequence Data; Nitrates; Oxidation-Reduction; Piperazines; Spectrum Analysis; Streptomyces; Tryptophan | 2012 |
MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.
Topics: Crystallography, X-Ray; Electron Transport; Endopeptidases; Heme; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Tryptophan | 2013 |
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.
Topics: Catalysis; Electron Transport; Heme; Indolequinones; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan | 2013 |
MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.
Topics: Bacteria; Electron Transport; Heme; Heme Oxygenase (Decyclizing); Indolequinones; Models, Molecular; Peroxidase; Tryptophan | 2014 |
Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG.
Topics: Antitubercular Agents; Archaea; Bacteria; Bacterial Proteins; Catalase; Coenzymes; Heme; Isoniazid; Methionine; Models, Molecular; Mycobacterium tuberculosis; Peroxidase; Prodrugs; Tryptophan; Tyrosine | 2014 |
Heme-dependent dioxygenases in tryptophan oxidation.
Topics: Animals; Heme; Humans; Hydrogen Peroxide; Models, Molecular; Oxygen; Tryptophan; Tryptophan Oxygenase | 2014 |
Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
Topics: Amino Acids; Coenzymes; Dipeptides; Electron Transport; Heme; Humans; Indolequinones; Lysine; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Processing, Post-Translational; Quinones; Tryptophan | 2018 |
Hypothesis: Metabolic targeting of 5-aminolevulinate synthase by tryptophan and inhibitors of heme utilisation by tryptophan 2,3-dioxygenase as potential therapies of acute hepatic porphyrias.
Topics: 5-Aminolevulinate Synthetase; Allopurinol; Animals; Enzyme Induction; Enzyme Inhibitors; Fasting; Feedback, Physiological; Gene Silencing; Glucose; Guinea Pigs; Heme; Humans; Kynurenine; Liver; Models, Biological; Molecular Targeted Therapy; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; Porphyrias, Hepatic; Rodentia; Species Specificity; Tryptophan; Tryptophan Oxygenase | 2019 |
254 other study(ies) available for heme and tryptophan
| Article | Year |
|---|---|
Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group.
Topics: Cytochrome c Group; Energy Transfer; Fluorescence; Guanidines; Heme; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Temperature; Tryptophan; Tyrosine; Urea | 1976 |
Isolation, crystallization, and properties of indolyl-3-alkane alpha-hydroxylase. A novel tryptophan-metabolizing enzyme.
Topics: Amino Acids; Animals; Chromatography, Gas; Crystallization; Heme; Hemeproteins; Hydrogen-Ion Concentration; Indoles; Iron; Kinetics; Magnetic Resonance Spectroscopy; Mass Spectrometry; Mice; Mixed Function Oxygenases; Molecular Weight; Pseudomonas; Spectrophotometry; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Tryptophan | 1977 |
On the molecular conformation of human haemopexin. I. Reactivity of the tyrosine and tryptophan side chains.
Topics: Circular Dichroism; Heme; Hemopexin; Humans; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Spectrophotometry; Tryptophan; Tyrosine | 1977 |
1H NMR studies at 360 MHz of the aromatic amino acid residues in ferrocytochrome c-552 from Euglena gracilis.
Topics: Animals; Binding Sites; Cytochrome c Group; Euglena gracilis; Heme; Iron; Magnetic Resonance Spectroscopy; Protein Binding; Protein Conformation; Tryptophan; Tyrosine | 1977 |
Modification of cytochrome c: modification of aromatic amino acids, photoaffinity labels, and metal substitution.
Topics: Affinity Labels; Amino Acids; Animals; Cations, Divalent; Chemical Phenomena; Chemistry; Cytochrome c Group; Formates; Heme; Horses; Myocardium; Photochemistry; Porphyrins; Tryptophan; Tyrosine | 1978 |
Regulation of rat liver tryptophan pyrrolase by its cofactor haem: Experiments with haematin and 5-aminolaevulinate and comparison with the substrate and hormonal mechanisms.
Topics: Aminolevulinic Acid; Apoenzymes; Cycloheximide; Dactinomycin; Hematinics; Heme; Hydrocortisone; Liver; Porphyrias; Porphyrinogens; Puromycin; Tryptophan; Tryptophan Oxygenase | 1975 |
Rates of energy transfer between tryptophans and hemes in hemoglobin, assuming that the heme is a planar oscillator.
Topics: Energy Transfer; Heme; Hemoglobins; Humans; Mathematics; Models, Molecular; Oscillometry; Oxyhemoglobins; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan | 1992 |
Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome c Group; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Heme; Kinetics; Mathematics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligonucleotide Probes; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry; Tryptophan | 1991 |
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
Topics: Amino Acids; Cytochrome c Group; Cytochromes c; Heme; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Tryptophan; Tyrosine | 1991 |
Quenching of tryptophan phosphorescence in Escherichia coli alkaline phosphatase by long-range transfer mechanisms to external agents in the rapid-diffusion limit.
Topics: Alkaline Phosphatase; Azo Compounds; Cytochrome c Group; Diffusion; Electron Transport; Electronic Data Processing; Escherichia coli; Fluorescent Dyes; Heme; Indicators and Reagents; Luminescent Measurements; Myoglobin; Tryptophan | 1991 |
Fluorescence decay kinetics of the tryptophyl residues of myoglobin: effect of heme ligation and evidence for discrete lifetime components.
Topics: Animals; Chromatography, High Pressure Liquid; Heme; Hydrogen-Ion Concentration; Kinetics; Myoglobin; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Tuna; Whales | 1990 |
Myelin basic protein binds heme at a specific site near the tryptophan residue.
Topics: Animals; Binding Sites; Cattle; Heme; Kinetics; Models, Molecular; Myelin Basic Protein; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 1987 |
Acute hepatic heme depletion: impaired gluconeogenesis in rats.
Topics: Animals; Brain; Dicarbethoxydihydrocollidine; Gluconeogenesis; Glutathione; Glycerol; Heme; Hydroxyindoleacetic Acid; Liver; Phenobarbital; Porphyrias; Rats; Serotonin; Tryptophan; Tryptophan Oxygenase | 1989 |
Detection of an oxyferryl porphyrin pi-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I.
Topics: Crystallization; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Hydrogen Peroxide; Mutation; Peroxidases; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet; Tryptophan | 1989 |
Magnetic circular dichroism studies on the heme and tryptophan components of cytochrome c peroxidase.
Topics: Cyanides; Cytochrome-c Peroxidase; Fluorides; Heme; Horseradish Peroxidase; Peroxidases; Tryptophan | 1985 |
Purification and characterization of tryptophan dioxygenase from Streptomyces parvulus.
Topics: Heme; Kinetics; Molecular Weight; Streptomyces; Substrate Specificity; Tryptophan; Tryptophan Oxygenase | 1988 |
Depletion of liver regulatory heme in benzene exposed rats.
Topics: 5-Aminolevulinate Synthetase; Animals; Benzene; Female; Heme; Liver; Porphobilinogen Synthase; Rats; Tryptophan; Tryptophan Oxygenase | 1988 |
Tryptophan 2,3-dioxygenase in chick embryo hepatocytes: studies in ovo and in culture.
Topics: Animals; Cells, Cultured; Chick Embryo; Cytochrome P-450 Enzyme System; Glutethimide; Heme; Hydrogen-Ion Concentration; Kinetics; Kynurenine; Liver; Male; Methemoglobin; Rats; Rats, Inbred Strains; Tryptophan; Tryptophan Oxygenase | 1988 |
Drug-induced modulations of hepatic heme metabolism. Neurological consequences.
Topics: Animals; Brain; Gastric Emptying; Gluconeogenesis; Heme; Intestine, Small; Liver; Liver Diseases; Models, Biological; Porphyrias; Pyrimethamine; Rats; Serotonin; Tryptophan | 1987 |
Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin.
Topics: Animals; Fluorescence Polarization; Heme; Hemeproteins; Metmyoglobin; Models, Chemical; Protein Conformation; Thermodynamics; Tryptophan; Whales | 1987 |
Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques.
Topics: Amino Acid Sequence; Animals; Heme; Macromolecular Substances; Magnetic Resonance Spectroscopy; Myoglobin; Tryptophan; Tyrosine; Whales | 1987 |
Oxidation of tryptophans in an interhelical hydrophobic cluster of myoglobin alters the thermodynamics of the denaturation transition.
Topics: Animals; Apoproteins; Heme; Hydrogen-Ion Concentration; Macromolecular Substances; Models, Molecular; Myoglobin; Oxidation-Reduction; Potentiometry; Protein Conformation; Protein Denaturation; Thermodynamics; Tryptophan; Whales | 1987 |
The role of haem in the regulation of rat liver tryptophan metabolism.
Topics: Animals; Heme; Hemin; Liver; Male; Rats; Rats, Inbred Strains; Tryptophan; Tryptophan Oxygenase | 1986 |
Elevated brain tryptophan and enhanced 5-hydroxytryptamine turnover in acute hepatic heme deficiency: clinical implications.
Topics: Animals; Brain; Cytochrome P-450 Enzyme Inhibitors; Disease Models, Animal; Heme; Liver; Liver Diseases; Male; Morphine; Porphyrias; Rats; Rats, Inbred Strains; Serotonin; Tryptophan | 1985 |
Energy-transfer study of cytochrome b5 using the anthroyloxy fatty acid membrane probes.
Topics: Animals; Cytochrome b Group; Cytochromes b5; Energy Transfer; Fluorescent Dyes; Heme; Liver; Membrane Proteins; Protein Binding; Rabbits; Spectrometry, Fluorescence; Spectrophotometry; Stearic Acids; Structure-Activity Relationship; Tryptophan | 1985 |
Redox state and chain folding in cytochrome c.
Topics: Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Biological Evolution; Cytochrome c Group; Fishes; Heme; Horses; Iron; Models, Structural; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Porphyrins; Protein Binding; Protein Conformation; Species Specificity; Tryptophan; Tyrosine | 1974 |
Electron transfer within and between haemoprotein molecules.
Topics: Amino Acid Oxidoreductases; Amino Acids; Blood Proteins; Cytochromes; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; In Vitro Techniques; Iron; Myoglobin; Oxidation-Reduction; Tryptophan; Tyrosine | 1965 |
Studies on the roles of the catalytic and allosteric sites in modulating the reactivity of tryptophan oxygenase with heme ligands. I. Cyanide derivatives.
Topics: Allosteric Regulation; Binding Sites; Catalysis; Chemical Phenomena; Chemistry, Physical; Cyanides; Electron Spin Resonance Spectroscopy; Fluorine; Guanidines; Heme; Hydrochloric Acid; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Nitriles; Oxidation-Reduction; Peroxidases; Plants; Potassium; Protein Binding; Protein Conformation; Protein Denaturation; Pseudomonas; Spectrophotometry; Sulfites; Tryptophan; Tryptophan Oxygenase | 1971 |
Selective cleavage of the single tryptophanyl peptide bond in horse heart cytochrome c.
Topics: Amino Acids; Animals; Autoanalysis; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Thin Layer; Cytochrome c Group; Disulfides; Heme; Horses; Myocardium; Peptides; Protein Conformation; Skatole; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfenic Acids; Tryptophan | 1973 |
Studies of the copper and heme cofactors of pseudomonad L-tryptophan-2,3-dioxygenase by electron paramagnetic resonance spectroscopy.
Topics: Allosteric Regulation; Ascorbic Acid; Binding Sites; Chromatography, Gel; Copper; Cyanides; Dialysis; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Ferricyanides; Heme; Oxidation-Reduction; Protein Binding; Protein Denaturation; Pseudomonas; Spectrophotometry, Ultraviolet; Tryptophan; Tryptophan Oxygenase; Ultrafiltration | 1973 |
The mechanism of inhibition of rat liver tryptophan pyrrolase activity by 4-hydroxypyrazolo(3,4-d)pyrimidine (Allopurinol).
Topics: Allopurinol; Alloxan; Animals; Ascorbic Acid; Cyclic AMP; Ethanol; Heme; Hydrocortisone; Hypoxanthines; Injections, Intraperitoneal; Liver; Male; NAD; Rats; Tryptophan; Tryptophan Oxygenase; Xanthine Oxidase; Xanthines | 1973 |
Spectroscopic studies on the conformation of cytochrome c and apocytochrome c.
Topics: Animals; Apoproteins; Chemical Phenomena; Chemistry; Computers; Cytochrome c Group; Deuterium; Fluorescence; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myocardium; Osmolar Concentration; Protein Conformation; Protein Denaturation; Protons; Sodium Chloride; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan; Viscosity | 1974 |
The purification and amino acid sequence of cytochrome C-552 from Euglena gracilis.
Topics: Amino Acid Sequence; Centrifugation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cysteine; Cytochrome c Group; Cytochromes; Electrophoresis, Polyacrylamide Gel; Euglena gracilis; Heme; Hydroxylamines; Mitochondria; Tryptophan | 1974 |
Proton magnetic resonances in cytochrome b2 core. Structural similarities with cytochrome b5.
Topics: Cytochromes; Deuterium; Heme; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Saccharomyces cerevisiae; Tryptophan | 1973 |
Purification and properties of rat liver tryptophan oxygenase.
Topics: Amino Acids; Animals; Chemical Precipitation; Chromatography, Ion Exchange; Cortisone; Electrophoresis, Disc; Heme; Hot Temperature; Hydrogen-Ion Concentration; Immunodiffusion; Liver; Macromolecular Substances; Male; Molecular Weight; Oxidation-Reduction; Rabbits; Rats; Sodium Dodecyl Sulfate; Spectrophotometry; Tryptophan; Tryptophan Oxygenase; Ultracentrifugation | 1972 |
On the role of copper in activation of and catalysis by tryptophan-2,3-dioxygenase.
Topics: Animals; Ascorbic Acid; Binding, Competitive; Catalysis; Chelating Agents; Copper; Enzyme Activation; Heme; Iron; Kinetics; Liver; Macromolecular Substances; Models, Chemical; Phenanthrolines; Pseudomonas; Rats; Species Specificity; Sulfonic Acids; Thiocarbamates; Tryptophan; Tryptophan Oxygenase | 1972 |
Tryptophan pyrrolase in rat liver after phenobarbital administration.
Topics: Animals; Ascorbic Acid; Dactinomycin; Enzyme Activation; Enzyme Induction; Heme; Hydrocortisone; Liver; Male; Phenobarbital; Proteins; Rats; Time Factors; Tryptophan; Tryptophan Oxygenase | 1973 |
The effects of chemical porphyrogens and drugs on the activity of rat liver tryptophan pyrrolase.
Topics: Acetamides; Allylisopropylacetamide; Animals; Apoproteins; Cytochrome P-450 Enzyme System; Dicarboxylic Acids; Griseofulvin; Heme; Humans; Hydrocortisone; Levulinic Acids; Liver; Male; Mental Disorders; Microsomes; Phenobarbital; Phenylbutazone; Porphyrias; Proadifen; Protein Precursors; Pyridines; Rats; Starvation; Time Factors; Tryptophan; Tryptophan Oxygenase | 1973 |
Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin.
Topics: Arginine; Australia; Chemical Phenomena; Chemistry; Circular Dichroism; Globins; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Inositol; Macromolecular Substances; Magnetic Resonance Spectroscopy; Magnetics; Mutation; Organophosphorus Compounds; Oxygen; Oxyhemoglobins; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Succinimides; Tryptophan; Tyrosine; X-Ray Diffraction | 1974 |
Modification of tryptophan residues of rabbit hemopexin by N-bromosuccinimide.
Topics: Animals; Apoproteins; Chemical Phenomena; Chemistry; Circular Dichroism; Heme; Hemopexin; Hydrogen-Ion Concentration; Oxidation-Reduction; Protein Binding; Protein Conformation; Rabbits; Spectrophotometry; Succinimides; Temperature; Tryptophan | 1974 |
Studies on the roles of synthesis and degradation in the control of enzyme levels in animal tissues.
Topics: Animals; Arginase; Cortisone; Heme; Homeostasis; Hydrocortisone; Immunodiffusion; Leucine; Liver; Lysine; Oxygenases; Rats; Transaminases; Tryptophan; Tryptophan Oxygenase; Ultracentrifugation | 1966 |
Studies on the genetic control of tryptophan pyrrolase in Drosophila melanogaster.
Topics: Alleles; Chromatography; Drosophila melanogaster; Genes; Genes, Recessive; Heme; Methemoglobin; Molecular Weight; Mutation; Sex Factors; Suppression, Genetic; Time Factors; Tryptophan; Tryptophan Oxygenase | 1971 |
The effects of allosteric interaction on the kinetics, spectra, and tertiary structure of pseudomonad tryptophan oxygenase.
Topics: Allosteric Regulation; Binding Sites; Catalysis; Chemical Phenomena; Chemistry; Detergents; Drug Stability; Fluorine; Heme; Iron; Kinetics; Oxygen; Protein Binding; Protein Conformation; Pseudomonas; Spectrophotometry; Sulfuric Acids; Tryptophan; Tryptophan Oxygenase; Ultraviolet Rays | 1972 |
Interaction of rose bengal with apo-hemoproteins. An essential histidine residue in cytochrome c peroxidase.
Topics: Apoproteins; Binding Sites; Cytochromes; Heme; Hemoglobins; Histidine; Hydrogen Peroxide; Kinetics; Myoglobin; Peroxidases; Photochemistry; Rose Bengal; Spectrophotometry; Tryptophan | 1972 |
The effect of heme binding on the tryptophan residue and the protein conformation of cytochrome b 5 .
Topics: 1-Propanol; Acetates; Acylation; Anhydrides; Animals; Apoproteins; Cattle; Circular Dichroism; Cytochromes; Ethanol; Heme; Mathematics; Protein Binding; Protein Conformation; Protein Denaturation; Rabbits; Spectrometry, Fluorescence; Spectrophotometry; Tryptophan; Ultracentrifugation; Ultraviolet Rays; Urea | 1972 |
Probing the topography of proteins in solution by photosensitized oxidation. The heme environment in horse heart ferrocytochrome c.
Topics: Amino Acids; Animals; Chromatography, Gel; Cyanides; Cytochromes; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Light; Methionine; Myocardium; Oxidation-Reduction; Peptides; Photochemistry; Radiation Effects; Tryptophan; Tyrosine | 1971 |
Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-L-tryptophan n-hexyl ester.
Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Cold Temperature; Cyclohexanes; Cytochromes; Energy Transfer; Esters; Glycerol; Heme; Horses; Hydrogen-Ion Concentration; Indoles; Isoenzymes; Myocardium; Peroxidases; Phenylalanine; Plants; Spectrophotometry; Stearic Acids; Tryptophan; Tyrosine; Ultraviolet Rays | 1971 |
Studies on the catalytic and allosteric sites in modulating the reactivity of tryptophan oxygenase with heme ligands. II. Carbon monoxide derivatives.
Topics: Allosteric Regulation; Binding Sites; Carbon Monoxide; Catalysis; Chemical Phenomena; Chemistry; Fluorine; Heme; Hydrogen-Ion Concentration; Kinetics; Models, Biological; Oxidation-Reduction; Protein Binding; Protein Conformation; Pseudomonas; Spectrophotometry; Sulfites; Tryptophan; Tryptophan Oxygenase | 1971 |
Electrical conductivity of some organic materials containing metals.
Topics: Cobalt; Copper; Cytochromes; Electric Conductivity; Electron Transport; Heme; Iron; Organometallic Compounds; Proteins; Tryptophan; Tyrosine | 1971 |
Electronic aspects of catalysis of the oxygenases.
Topics: Catalysis; Catechols; Dialysis; Electrons; Heme; Hemoglobins; Methods; Molecular Weight; Oxygen; Oxygenases; Proteins; Spectrum Analysis; Tryptophan | 1969 |
Inhibitory effects of phenylhydrazine on the induction of tryptophan pyrrolase in rats.
Topics: Adrenal Glands; Adrenalectomy; Animals; Depression, Chemical; Enzyme Induction; Heme; Hydrocortisone; Liver; Male; Methemoglobin; Nitrites; Phenylhydrazines; Porphyrins; Rats; Stimulation, Chemical; Time Factors; Tryptophan; Tryptophan Oxygenase | 1970 |
Acid denaturation of carbonylhemoglobin. Protein unfolding without heme detachment.
Topics: Animals; Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry; Heme; Hemoglobins; Horses; Humans; Hydrogen-Ion Concentration; Kinetics; Optical Rotatory Dispersion; Protein Denaturation; Tryptophan; Ultraviolet Rays | 1970 |
The oxygenated form of L-tryptophan 2,3-dioxygenase as reaction intermediate.
Topics: Chemical Phenomena; Chemistry; Chromatography, DEAE-Cellulose; Chromatography, Gel; Heme; Iron; Kinetics; Kynurenine; Oxygen; Protein Binding; Pseudomonas; Spectrophotometry; Tryptophan; Tryptophan Oxygenase | 1970 |
Fluorescence studies of Aplysia and sperm whale apomyoglobins.
Topics: Animals; Binding Sites; Cetacea; Chemical Phenomena; Chemistry; Fluorescence; Heme; Hemoglobins; Humans; Mollusca; Myoglobin; Naphthalenes; Rotation; Spectrophotometry; Sulfonic Acids; Tryptophan; Water | 1970 |
Structural location of the tyrosyl and tryptophanyl residues of tuna heart cytochrome c.
Topics: Amino Acid Sequence; Animals; Chemical Phenomena; Chemistry; Cytochromes; Diiodotyrosine; Fishes; Heme; Hydrogen-Ion Concentration; Iodine; Iron; Monoiodotyrosine; Myocardium; Oxidation-Reduction; Solvents; Spectrophotometry; Tryptophan; Tyrosine; Ultraviolet Rays | 1970 |
Fluorescence and phosphorescence of yeast L-lactate dehydrogenase (cytochrome b2). Relative orientations of the prosthetic heme and flavin.
Topics: Chemical Phenomena; Chemistry; Cytochromes; Energy Transfer; Flavin Mononucleotide; Fluorescence; Fluorometry; Heme; L-Lactate Dehydrogenase; Luminescent Measurements; Mathematics; Models, Structural; Porphyrins; Protein Binding; Saccharomyces; Temperature; Tryptophan | 1971 |
Purification and characterization of cytochrome 553 from the chrysophycean alga Monochrysis lutheri.
Topics: Amino Acids; Arginine; Autoanalysis; Chemical Precipitation; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Cytochromes; Dialysis; Electron Transport; Electrophoresis, Disc; Eukaryota; Freeze Drying; Heme; Histidine; Iron; Isoelectric Focusing; Methionine; Methods; Molecular Weight; Oxidation-Reduction; Photosynthesis; Proline; Quaternary Ammonium Compounds; Spectrophotometry; Sulfates; Tryptophan; Ultracentrifugation; Ultraviolet Rays | 1971 |
Studies on the interaction of carbon monoxide with tryptophan oxygenase of Pseudomonas.
Topics: Ascorbic Acid; Binding Sites; Carbon Monoxide; Heme; Iron; Kinetics; Light; Oxygen; Porphyrins; Protein Binding; Pseudomonas; Tryptophan; Tryptophan Oxygenase | 1968 |
Type c ferri- and ferrohemochrome formation between hemin c, amino acids, and peptides.
Topics: Amino Acids; Ammonia; Arginine; Cytochromes; Detergents; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Indoles; Iron; Lysine; Methionine; Peptides; Pigments, Biological; Porphyrins; Protein Binding; Spectrophotometry; Sulfur; Tryptophan | 1968 |
Peroxidase isoenzymes from horseradish roots. 3. Circular dichroism of isoenzymes and apoisoenzymes.
Topics: Binding Sites; Heme; Isoenzymes; Peroxidases; Phenylalanine; Plants; Spectrophotometry; Spectrum Analysis; Tryptophan; Tyrosine; Ultraviolet Rays | 1968 |
Inhibition of tryptophan pyrrolase induction by carbon tetrachloride in rats.
Topics: Animals; Carbon Tetrachloride Poisoning; Chemical and Drug Induced Liver Injury; Enzyme Induction; Female; Heme; Hydrocortisone; Liver; Rats; Time Factors; Tryptophan; Tryptophan Oxygenase | 1968 |
Effect of yohimbine on tryptophan metabolism.
Topics: Adrenal Glands; Adrenalectomy; Animals; Carbon Dioxide; Carbon Isotopes; Depression, Chemical; Heme; Male; Pyrroles; Rats; Tryptophan; Tryptophan Oxygenase; Yohimbine | 1969 |
Solvent perturbation studies of heme proteins and other colored proteins.
Topics: Animals; Catalase; Cattle; Cetacea; Cytochromes; Deuterium; Glycerol; Glycols; Heme; Hemoglobins; Horses; Hydrogen-Ion Concentration; Liver; Myoglobin; Optical Rotatory Dispersion; Solvents; Spectrum Analysis; Sucrose; Tryptophan; Tyrosine; Ultraviolet Rays; Urea; Water | 1969 |
Optical rotatory dispersion of human hemoglobins A, F, S, C, and M.
Topics: Chemical Phenomena; Chemistry; Fetal Hemoglobin; Genes; Heme; Hemoglobin C; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Methemoglobin; Optical Rotatory Dispersion; Oxidation-Reduction; Spectrophotometry; Temperature; Tryptophan; Tyrosine | 1969 |
Photodynamic action of porphyrins on amino acids and proteins. I. Selective photooxidation of methionine in Aqueous solution.
Topics: Amino Acids; Chemical Phenomena; Chemistry; Chlorophyll; Hematoporphyrins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Light; Magnesium; Methionine; Micrococcus; Muramidase; Oxidation-Reduction; Porphyrins; Radiation Effects; Spectrophotometry; Time Factors; Tryptophan; Tyrosine; Water | 1969 |
On the activation and catalytic mechanism of microbial tryptophan pyrrolase.
Topics: Ascorbic Acid; Catalysis; Heme; In Vitro Techniques; Kynurenine; Oxygenases; Pseudomonas; Tryptophan; Tryptophan Oxygenase | 1964 |
Tryptophan pyrrolase of liver. I. Activation and assay in soluble extracts of rat liver.
Topics: Animals; Catalysis; Heme; Hydrocortisone; In Vitro Techniques; Liver; Methemoglobin; Oxygenases; Rats; Subcellular Fractions; Tryptophan; Tryptophan Oxygenase | 1966 |
Fluorometric and spectrophotometric study of heme binding on the apoprotein from a cytochrome b-2-derivative.
Topics: Coenzymes; Cytochromes; Flavins; Fluorometry; Heme; L-Lactate Dehydrogenase; Protein Binding; Spectrophotometry; Trypsin; Tryptophan; Tyrosine; Urea | 1967 |
Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes.
Topics: Amidohydrolases; Ascorbic Acid; Carbon Monoxide; Catalysis; Cyanides; Heme; Intestine, Small; Intestines; Kinetics; Kynurenine; Light; Methylene Blue; Spectrophotometry; Tryptophan; Tryptophan Oxygenase | 1967 |
The structural environment of the tryptophanyl residue of horse heart ferricytochrome c.
Topics: Amino Acids; Animals; Cytochromes; Heme; Horses; Hydrogen-Ion Concentration; Methionine; Myocardium; Oxidation-Reduction; Spectrophotometry; Tryptophan; Tyrosine; Viscosity | 1967 |
Extensive studies of the heme coordination structure of indoleamine 2,3-dioxygenase and of tryptophan binding with magnetic and natural circular dichroism and electron paramagnetic resonance spectroscopy.
Topics: Animals; Circular Dichroism; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Hydrogen-Ion Concentration; Intestine, Small; Oxygenases; Rabbits; Tryptophan; Tryptophan Oxygenase | 1984 |
Location of the heme groups in cytochrome cd1 oxidase from Pseudomonas aeruginosa.
Topics: Electron Transport Complex IV; Heme; Kinetics; Molecular Weight; Protein Binding; Protein Conformation; Pseudomonas aeruginosa; Spectrometry, Fluorescence; Tryptophan; X-Ray Diffraction | 1980 |
Structure and heme environment of ferrocytochrome c553 from 1H NMR studies.
Topics: Cyanobacteria; Cytochrome c Group; Heme; Histidine; Magnetic Resonance Spectroscopy; Methionine; Phenylalanine; Protein Conformation; Tryptophan; Tyrosine | 1982 |
Picosecond fluorescence decay of tryptophans in myoglobin.
Topics: Animals; Apoproteins; Energy Transfer; Fluorescence Polarization; Heme; Mathematics; Metmyoglobin; Myoglobin; Time Factors; Tryptophan; Tuna; Whales | 1984 |
Defective utilization of haem in selenium-deficient rat liver.
Topics: Allylisopropylacetamide; Animals; Heme; Liver; Male; Microsomes, Liver; Rats; Selenium; Tryptophan; Tryptophan Oxygenase | 1983 |
Intramolecular tryptophan heme energy transfer in horseradish peroxidase.
Topics: Energy Transfer; Heme; Horseradish Peroxidase; Peroxidases; Spectrometry, Fluorescence; Tryptophan | 1983 |
L-tryptophan: a common denominator of biochemical and neurological events of acute hepatic porphyria?
Topics: Animals; Brain; Heme; Liver; Liver Diseases; Male; Nervous System Diseases; Porphyrias; Rats; Rats, Inbred Strains; Serotonin; Tryptophan; Tryptophan Oxygenase | 1983 |
Activation of liver tryptophan oxygenase by hydrocortisone, hematin and tryptophan in streptozotocin-diabetic rats.
Topics: Animals; Apoenzymes; Diabetes Mellitus, Experimental; Enzyme Activation; Heme; Hemin; Hydrocortisone; Male; Rats; Rats, Inbred Strains; Tryptophan; Tryptophan Oxygenase | 1984 |
Epinephrine and other activators of prostaglandin endoperoxide synthetase can reduce Fe3+-heme to Fe2+-heme.
Topics: Ascorbic Acid; Chemical Phenomena; Chemistry; Enzyme Activation; Epinephrine; Ferric Compounds; Ferrous Compounds; Heme; Lipoxygenase; Oxidation-Reduction; Tryptophan | 1980 |
Tryptophan and tryptophan pyrrolase in haem regulation. The role of lipolysis and direct displacement of serum-protein-bound tryptophan in the opposite effects of administration of endotoxin, morphine, palmitate, salicylate and theophylline on rat liver 5
Topics: 5-Aminolevulinate Synthetase; Animals; Carboxylic Acids; Endotoxins; Heme; Lipolysis; Lipopolysaccharides; Liver; Male; Morphine; Rats; Rats, Inbred Strains; Theophylline; Tryptophan; Tryptophan Oxygenase | 1982 |
Tryptophan pyrrolase in haem regulation. The mechanism of the opposite effects of tryptophan on rat liver 5-aminolaevulinate synthase activity and the haem saturation of tryptophan pyrrolase.
Topics: 5-Aminolevulinate Synthetase; Animals; Dose-Response Relationship, Drug; Female; Heme; Lead; Liver; Male; Organometallic Compounds; Rats; Rats, Inbred Strains; Tryptophan; Tryptophan Oxygenase | 1981 |
Refolding defects in hemoglobin Rothschild.
Topics: Absorption; Circular Dichroism; Globins; Heme; Hemoglobins, Abnormal; Humans; Protein Conformation; Spectrum Analysis; Tryptophan | 1980 |
Tryptophan-heme energy transfer in human hemoglobin: dependence upon the state of the iron.
Topics: Adult; Binding Sites; Computers; Heme; Hemoglobin A; Humans; Iron; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 1980 |
Secondary and tertiary structure of the A-state of cytochrome c from resonance Raman spectroscopy.
Topics: Animals; Crystallography, X-Ray; Cytochrome c Group; Heme; Horses; Hydrogen Bonding; Iron; Models, Molecular; Molecular Structure; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrum Analysis, Raman; Thermodynamics; Tryptophan; Tyrosine | 1995 |
Tryptophan 2,3-dioxygenase in Saccharomyces cerevisiae.
Topics: Azides; Binding Sites; Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Isoelectric Point; Kynurenine; Potassium Cyanide; Saccharomyces cerevisiae; Sodium Azide; Substrate Specificity; Tryptophan; Tryptophan Oxygenase | 1995 |
pH-induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes.
Topics: Cyanides; Energy Transfer; Fluorescence; Heme; Horseradish Peroxidase; Hydrogen Bonding; Hydrogen-Ion Concentration; Molecular Structure; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 1995 |
The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.
Topics: Alanine; Bacillus megaterium; Bacterial Proteins; Base Sequence; Catalysis; Circular Dichroism; Cytochrome P-450 Enzyme System; DNA Primers; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Heme; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Phenylalanine; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 1994 |
Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization.
Topics: Alanine; Aspartic Acid; Base Sequence; Binding Sites; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Temperature; Tryptophan | 1994 |
Effect of disordered hemes on energy transfer rates between tryptophans and heme in myoglobin.
Topics: Animals; Biophysical Phenomena; Biophysics; Carboxyhemoglobin; Energy Transfer; Heme; Hemoglobins; In Vitro Techniques; Methemoglobin; Myoglobin; Spectrophotometry; Tryptophan; Whales | 1993 |
Reaction of horse cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I.
Topics: Animals; Cytochrome c Group; Cytochrome-c Peroxidase; Free Radicals; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Osmolar Concentration; Oxidation-Reduction; Photolysis; Recombinant Proteins; Tryptophan | 1994 |
Decreased nocturnal plasma melatonin levels in patients with recurrent acute intermittent porphyria attacks.
Topics: Adult; Arginine; Circadian Rhythm; Female; Heme; Humans; Melatonin; Porphyria, Acute Intermittent; Recurrence; Tryptophan | 1993 |
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
Topics: Aspartic Acid; Binding Sites; Crystallography; Cytochrome-c Peroxidase; DNA Mutational Analysis; Electron Spin Resonance Spectroscopy; Ferric Compounds; Free Radicals; Heme; Histidine; Hydrogen Bonding; In Vitro Techniques; Kinetics; Models, Molecular; Oxidation-Reduction; Recombinant Proteins; Structure-Activity Relationship; Tryptophan; X-Ray Diffraction | 1993 |
Protein and amino acid oxidation is associated with increased chemiluminescence.
Topics: Antioxidants; Deferoxamine; Dimethyl Sulfoxide; Ethylamines; Heme; Histidine; Kinetics; Luminescent Measurements; Oxidation-Reduction; Oxygen Consumption; Peroxides; Piperazines; Pyridines; Serum Albumin, Bovine; Superoxide Dismutase; tert-Butylhydroperoxide; Tryptophan; Tyrosine | 1993 |
Comparative effects of heme and metalloporphyrins on interferon-gamma-mediated pathways in monocytic cells (THP-1).
Topics: Biopterins; Heme; HLA-DR Antigens; Humans; Interferon-gamma; Kinetics; Leukemia, Monocytic, Acute; Metalloporphyrins; Neopterin; Recombinant Proteins; Tryptophan; Tryptophan Oxygenase; Tumor Cells, Cultured | 1993 |
Increased delta aminolevulinic acid and decreased pineal melatonin production. A common event in acute porphyria studies in the rat.
Topics: Acetylserotonin O-Methyltransferase; Adrenergic alpha-Agonists; Adrenergic beta-Agonists; Aminolevulinic Acid; Animals; Arylamine N-Acetyltransferase; Cells, Cultured; Enzyme Inhibitors; gamma-Aminobutyric Acid; Heme; Heptanoates; In Vitro Techniques; Isoproterenol; Male; Melatonin; Norepinephrine; Photoperiod; Pineal Gland; Porphobilinogen Synthase; Porphyria, Acute Intermittent; Rats; Rats, Wistar; Tryptophan | 1996 |
Enzymatic and electron transfer activities in crystalline protein complexes.
Topics: Bacterial Proteins; Binding Sites; Copper; Crystallization; Cytochrome c Group; Electron Transport; Heme; Indolequinones; Macromolecular Substances; Models, Structural; Oxidoreductases Acting on CH-NH Group Donors; Protein Structure, Secondary; Quinones; Spectrophotometry; Tryptophan | 1996 |
Heme-CO binding to tryptophan-containing calmodulin mutants.
Topics: Animals; Binding Sites; Calmodulin; Carbon Monoxide; Cattle; Energy Transfer; Heme; Models, Molecular; Mutation; Protein Binding; Spectrometry, Fluorescence; Trifluoperazine; Tryptophan | 1996 |
A tryptophan pyrrole-ring cleavage enzyme in the most primitive eukaryote.
Topics: Animals; Chromatography, Ion Exchange; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Enzyme Inhibitors; Heme; Liver; Mammals; Molecular Weight; Pseudomonas; Saccharomyces cerevisiae; Substrate Specificity; Tryptophan; Tryptophan Oxygenase | 1996 |
Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase.
Topics: 2,2'-Dipyridyl; Cations; Coordination Complexes; Cytochrome c Group; Cytochrome-c Peroxidase; Electron Transport; Heme; Mutagenesis; Photochemistry; Photolysis; Ruthenium; Saccharomyces cerevisiae; Tryptophan | 1996 |
Submillisecond protein folding kinetics studied by ultrarapid mixing.
Topics: Animals; Cytochrome c Group; Fluorescence; Guanidine; Guanidines; Heme; Horses; Imidazoles; Kinetics; Myocardium; Protein Denaturation; Protein Folding; Tryptophan | 1997 |
Steady-state and picosecond-time-resolved fluorescence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450.
Topics: Bacillus megaterium; Bacterial Proteins; Binding Sites; Cytochrome P-450 Enzyme System; Energy Transfer; Escherichia coli; Heme; Mixed Function Oxygenases; Models, Molecular; Molecular Structure; NADPH-Ferrihemoprotein Reductase; Protein Conformation; Recombinant Proteins; Solvents; Spectrometry, Fluorescence; Tryptophan | 1997 |
Fluorescence studies of human semi-beta-hemoglobin assembly.
Topics: Apoproteins; Dimerization; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Models, Molecular; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 1998 |
A stable, molten-globule-like cytochrome c.
Topics: Circular Dichroism; Cytochrome c Group; Escherichia coli; Guanidine; Heme; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Proteins; Sequence Analysis; Thermus thermophilus; Tryptophan | 1998 |
Transmembrane heme delivery systems.
Topics: Amino Acid Sequence; ATP-Binding Cassette Transporters; Bacterial Proteins; Biological Transport; Cell Membrane; Chloroplasts; Heme; Hemeproteins; Histidine; Membrane Proteins; Molecular Sequence Data; Nuclear Proteins; Plant Proteins; Proteins; Protozoan Proteins; Recombinant Proteins; Sequence Alignment; Structure-Activity Relationship; Tryptophan | 1998 |
Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp).
Topics: Blood Substitutes; Crystallization; Crystallography, X-Ray; Heme; Hemoglobin A; Hemoglobins; Humans; Hydrogen Bonding; Ligands; Models, Molecular; Oxygen; Protein Binding; Protein Conformation; Recombinant Proteins; Tryptophan; Valine; Water | 1998 |
Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences.
Topics: Amino Acid Sequence; Binding Sites; Conserved Sequence; Cystathionine beta-Synthase; Enzyme Activation; Heme; Hot Temperature; Humans; Hydrolysis; Molecular Sequence Data; Molecular Weight; Peptide Fragments; Protein Denaturation; Pyridoxal Phosphate; Recombinant Proteins; S-Adenosylmethionine; Solvents; Spectrometry, Fluorescence; Trypsin; Tryptophan | 1998 |
A test of the relationship between sequence and structure in proteins: excision of the heme binding site in apocytochrome b5.
Topics: Amino Acid Sequence; Animals; Apoproteins; Binding Sites; Circular Dichroism; Cytochrome b Group; Cytochromes b; Fluorescence; Heme; Liver; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis; Protein Denaturation; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Tryptophan | 1998 |
Time resolved emissions in the picosecond range of single tryptophan recombinant myoglobins reveal the presence of long range heme protein interactions.
Topics: Animals; Circular Dichroism; Heme; Myoglobin; Recombinant Proteins; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan; Whales | 1998 |
Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis.
Topics: Alcohol Oxidoreductases; Benzyl Alcohols; Binding Sites; Enzyme Stability; Escherichia coli; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Manganese; Mutagenesis, Site-Directed; Oxalates; Peroxidases; Phanerochaete; Recombinant Proteins; Solubility; Spectrophotometry; Substrate Specificity; Tryptophan | 1999 |
Engineering out motion: introduction of a de novo disulfide bond and a salt bridge designed to close a dynamic cleft on the surface of cytochrome b5.
Topics: Animals; Cytochromes b5; Disulfides; Heme; Hot Temperature; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Binding; Protein Denaturation; Protein Engineering; Rats; Salts; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Urea | 1999 |
Studies on the interactions between human serum albumin and imidazolium [trans-tetrachlorobis(imidazol)ruthenate(III)].
Topics: Bilirubin; Binding Sites; Circular Dichroism; Heme; Humans; Imidazoles; Immunochemistry; In Vitro Techniques; Organometallic Compounds; Protein Binding; Ruthenium; Serum Albumin; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Ultraviolet; Tryptophan; Warfarin | 1999 |
Ligand exchange during unfolding of cytochrome c.
Topics: Animals; Circular Dichroism; Cytochrome c Group; Guanidine; Heme; Horses; Kinetics; Ligands; Myocardium; Protein Denaturation; Protein Folding; Scattering, Radiation; Spectrometry, Fluorescence; Thermodynamics; Tryptophan | 1999 |
UV resonance Raman studies of alpha-nitrosyl hemoglobin derivatives: relation between the alpha 1-beta 2 subunit interface interactions and the Fe-histidine bonding of alpha heme.
Topics: Carboxyhemoglobin; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Histidine; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Models, Molecular; Phytic Acid; Protein Conformation; Spectrum Analysis, Raman; Tryptophan; Tyrosine; Ultraviolet Rays | 1999 |
Recombinant hemoglobin(alpha 29leucine --> phenylalanine, alpha 96valine --> tryptophan, beta 108asparagine --> lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation.
Topics: Amino Acid Substitution; Asparagine; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Humans; Kinetics; Leucine; Lysine; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Oxyhemoglobins; Phenylalanine; Protein Binding; Recombinant Proteins; Tryptophan; Valine | 1999 |
Structural and conformational stability of horseradish peroxidase: effect of temperature and pH.
Topics: Calcium; Circular Dichroism; Enzyme Stability; Guanidine; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Temperature; Tryptophan | 2000 |
A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins.
Topics: Biochemistry; Calorimetry; Cytochrome c Group; Heme; Hot Temperature; Hydrogen-Ion Concentration; Models, Chemical; Muramidase; Myoglobin; Protein Conformation; Protein Denaturation; Proteins; Ribonuclease, Pancreatic; Thermodynamics; Tryptophan; Tyrosine | 2000 |
Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis.
Topics: Amino Acid Substitution; Arginine; Electron Transport Complex IV; Heme; Histidine; Hydrogen Bonding; Mutagenesis, Site-Directed; Oxidation-Reduction; Paracoccus denitrificans; Propionates; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Tryptophan; Tyrosine | 2000 |
Two-state expansion and collapse of a polypeptide.
Topics: Animals; Computer Simulation; Cytochrome c Group; Diffusion; Guanidine; Heme; Horses; Kinetics; Lasers; Models, Chemical; Peptides; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tryptophan; Viscosity | 2000 |
Heme orientation affects holo-myoglobin folding and unfolding kinetics.
Topics: Animals; Apoproteins; Circular Dichroism; Dose-Response Relationship, Drug; Fluorescence; Guanidine; Heme; Horses; Kinetics; Metmyoglobin; Myoglobin; Protein Denaturation; Protein Folding; Protein Renaturation; Rotation; Thermodynamics; Tryptophan; Whales | 2000 |
Molecular basis for hyperactivity in tryptophan 409 mutants of neuronal NO synthase.
Topics: Amino Acid Substitution; Animals; Catalysis; Heme; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Rats; Recombinant Proteins; Spectrophotometry; Tryptophan; Tyrosine | 2000 |
Characterization of a structural model of membrane bound cytochrome c-550 from Bacillus subtilis.
Topics: Amino Acid Sequence; Animals; Bacillus subtilis; Cell Membrane; Circular Dichroism; Cytochrome c Group; Electrons; Heme; Horses; Kinetics; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Osmolar Concentration; Oxidation-Reduction; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Sequence Alignment; Spectrometry, Fluorescence; Static Electricity; Thermodynamics; Tryptophan | 2000 |
Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Catalase; Catalysis; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Heme; Leucine; Mass Spectrometry; Mutagenesis, Site-Directed; Peroxidases; Phenylalanine; Recombinant Proteins; Substrate Specificity; Tryptophan | 2000 |
Tryptophan-heme pi-electrostatic interactions in cytochrome f of oxygenic photosynthesis.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Chlamydomonas reinhardtii; Chloroplasts; Cyanobacteria; Cytochromes; Cytochromes f; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photosynthesis; Static Electricity; Tryptophan; Tyrosine | 2000 |
Aromatic residues and neighboring Arg414 in the (6R)-5,6,7, 8-tetrahydro-L-biopterin binding site of full-length neuronal nitric-oxide synthase are crucial in catalysis and heme reduction with NADPH.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Binding Sites; Biopterins; Catalysis; Dimerization; Drosophila; Glutamine; Heme; Humans; Hydrogen Bonding; Leucine; Mice; Models, Molecular; Molecular Sequence Data; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Rats; Spectrophotometry, Atomic; Structure-Activity Relationship; Tryptophan | 2000 |
Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c.
Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Electrochemistry; Electron Spin Resonance Spectroscopy; Enzyme Stability; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Structure-Activity Relationship; Tryptophan | 2000 |
Roles of Ile209 and Ile210 on the heme pocket structure and regulation of histidine kinase activity of oxygen sensor FixL from Rhizobium meliloti.
Topics: Bacterial Proteins; Carbon Monoxide; Enzyme Activation; Ferric Compounds; Heme; Hemeproteins; Histidine; Histidine Kinase; Isoleucine; Mutagenesis, Site-Directed; Oxygen; Phosphorylation; Protein Binding; Protein Conformation; Protein Kinases; Sinorhizobium meliloti; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tryptophan | 2000 |
Roles of the heme proximal side residues tryptophan409 and tryptophan421 of neuronal nitric oxide synthase in the electron transfer reaction.
Topics: Amino Acid Sequence; Animals; Binding Sites; Electron Transport; Heme; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Rabbits; Sequence Alignment; Tryptophan | 2000 |
Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
Topics: Amino Acid Substitution; Benzyl Alcohols; Catalysis; Crystallography, X-Ray; Escherichia coli; Heme; Hydrogen Bonding; Hydroxylation; Isoenzymes; Models, Molecular; Mutation; Oxidation-Reduction; Peroxidases; Phanerochaete; Protein Conformation; Recombinant Proteins; Tryptophan | 2001 |
Mutagenesis of key residues identifies the connection subdomain of HIV-1 reverse transcriptase as the site of inhibition by heme.
Topics: Heme; HIV Reverse Transcriptase; Metalloporphyrins; Microscopy, Fluorescence; Models, Molecular; Mutagenesis, Site-Directed; Oligopeptides; Protein Structure, Tertiary; Reverse Transcriptase Inhibitors; Tryptophan | 2001 |
Design, synthesis, and characterization of a novel hemoprotein.
Topics: Amino Acid Sequence; Circular Dichroism; Dose-Response Relationship, Drug; Heme; Hemeproteins; Kinetics; Molecular Sequence Data; Oxidation-Reduction; Peptide Biosynthesis; Protein Binding; Protein Conformation; Protein Denaturation; Protein Engineering; Software; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry; Temperature; Thermodynamics; Tryptophan | 2001 |
A proximal tryptophan in NO synthase controls activity by a novel mechanism.
Topics: Amino Acid Substitution; Cysteine; Heme; Hydrogen Bonding; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Protein Conformation; Recombinant Proteins; Spectrophotometry; Tryptophan | 2001 |
The role of distal tryptophan in the bifunctional activity of catalase-peroxidases.
Topics: Bacterial Proteins; Binding Sites; Catalysis; Cyanobacteria; Cytochrome-c Peroxidase; Escherichia coli; Heme; Hydrogen Peroxide; Kinetics; Multienzyme Complexes; Mutation; Oxidation-Reduction; Peroxidases; Protein Binding; Spectrophotometry; Tryptophan; Yeasts | 2001 |
Regulation of the properties of the heme-NO complexes in nitric-oxide synthase by hydrogen bonding to the proximal cysteine.
Topics: Cysteine; Heme; Hydrogen Bonding; Models, Molecular; Mutation; Nitric Oxide; Nitric Oxide Synthase; Protein Conformation; Spectrum Analysis, Raman; Tryptophan | 2001 |
Oxidative modification of tryptophan 43 in the heme vicinity of the F43W/H64L myoglobin mutant.
Topics: Catalysis; Chlorobenzoates; Chromatography, Liquid; Heme; Indicators and Reagents; Indoles; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutation; Myoglobin; Oxygen; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin; Tryptophan | 2001 |
A structural role for tryptophan 188 of inducible nitric oxide synthase.
Topics: Amino Acid Substitution; Animals; Circular Dichroism; Heme; Mice; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Phenylalanine; Protein Conformation; Spectrophotometry, Ultraviolet; Tryptophan | 2001 |
The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond.
Topics: Amino Acid Sequence; Amino Acids; Cloning, Molecular; Cross-Linking Reagents; Cysteine; Glutamic Acid; Heme; Indolequinones; Mass Spectrometry; Models, Chemical; Models, Genetic; Molecular Sequence Data; Open Reading Frames; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Protein Binding; Protein Processing, Post-Translational; Pseudomonas putida; Quinones; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfides; Tryptophan; X-Rays | 2001 |
A conserved tryptophan in nitric oxide synthase regulates heme-dioxy reduction by tetrahydrobiopterin.
Topics: Animals; Arginine; Biopterins; Conserved Sequence; Electron Spin Resonance Spectroscopy; Electrons; Heme; Kinetics; Light; Mice; Models, Chemical; Mutation; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Oxygen; Protein Binding; Spectrophotometry; Time Factors; Tryptophan | 2001 |
Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457.
Topics: Animals; Binding Sites; Biopterins; Catalysis; Conserved Sequence; Crystallography, X-Ray; Dimerization; Electron Transport; Escherichia coli; Heme; Hydrogen Bonding; Mice; Models, Chemical; Models, Molecular; Mutation; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Protein Binding; Recombinant Proteins; Tryptophan | 2001 |
Steady-state and picosecond time-resolved fluorescence studies on native and apo seed coat soybean peroxidase.
Topics: Entropy; Heme; Kinetics; Models, Chemical; Models, Molecular; Peroxidases; Plant Proteins; Spectrometry, Fluorescence; Time Factors; Tryptophan | 2001 |
Role of conformational changes in the heme-dependent regulation of human soluble guanylate cyclase.
Topics: Acrylamide; Circular Dichroism; Enzyme Activation; Guanylate Cyclase; Heme; Humans; Indazoles; Models, Chemical; Models, Molecular; Nitric Oxide; Nitric Oxide Donors; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan | 2001 |
A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.
Topics: Amino Acid Motifs; Amino Acid Sequence; Apoproteins; Bacterial Outer Membrane Proteins; Cytochrome c Group; Cytochromes c; DNA Primers; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Lyases; Models, Biological; Molecular Sequence Data; Mutation; Periplasm; Plasmids; Point Mutation; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Protein Transport; Tryptophan | 2002 |
Spectroscopic characterization of mutations at the Phe41 position in the distal haem pocket of horseradish peroxidase C: structural and functional consequences.
Topics: Amino Acid Substitution; Benzothiazoles; Heme; Horseradish Peroxidase; Isoenzymes; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Protein Binding; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Structure-Activity Relationship; Sulfonic Acids; Tryptophan; Valine | 2002 |
Time-resolved resonance Raman study on ultrafast structural relaxation and vibrational cooling of photodissociated carbonmonoxy myoglobin.
Topics: Animals; Heme; Horses; Myoglobin; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Time Factors; Tryptophan; Vibration | 2002 |
Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Biological Transport; Chlamydomonas; Chloroplasts; Conserved Sequence; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nuclear Proteins; Phenotype; Protozoan Proteins; Recombinant Fusion Proteins; Time Factors; Tryptophan | 2003 |
Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.
Topics: Acetylation; Amino Acid Substitution; Binding, Competitive; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins; Spectrometry, Fluorescence; Tryptophan | 2003 |
Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase.
Topics: Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Humans; Iron-Sulfur Proteins; Ligands; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Protein Structure, Tertiary; Solvents; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 2003 |
A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase.
Topics: Amino Acid Substitution; Cross-Linking Reagents; Crystallography, X-Ray; Cytochrome-c Peroxidase; Heme; Histidine; Imaging, Three-Dimensional; Models, Molecular; Mutation; Peroxides; Porphyrins; Protein Conformation; Protein Folding; Saccharomyces cerevisiae; Tryptophan; Tyrosine; Zinc | 2003 |
Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.
Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Blotting, Western; Catalysis; Cell Division; Circular Dichroism; Cytokines; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Interferon-gamma; Kinetics; Ligands; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Binding; Protein Conformation; Rats; Sequence Homology, Amino Acid; Tryptophan; Tryptophan Oxygenase; Ultraviolet Rays; Up-Regulation | 2003 |
MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis.
Topics: Amino Acid Sequence; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Indolequinones; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Sorting Signals; Quinones; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Tryptophan | 2003 |
THE ROLE OF COENZYMES, CORTISONE AND RNA IN THE CONTROL OF LIVER ENZYME LEVELS.
Topics: Adrenalectomy; Coenzymes; Cortisone; Dactinomycin; Heme; Hydro-Lyases; Liver; Metabolism; Peroxidases; Pharmacology; Puromycin; Rats; Research; RNA; Threonine; Transaminases; Tryptophan | 1963 |
INDUCTION OF HEME-PROTEIN ENZYME IN ANIMAL. II. INCREASED TURNOVER RATES OF RIBONUCLEIC ACID, PROTEIN AND HEME CAUSED BY THE SUBSTRATE ADMINISTRATION.
Topics: Amides; Amino Acids; Carbon Isotopes; Glycine; Heme; Hemeproteins; Hypnotics and Sedatives; Kynurenine; Liver; Peroxidases; Pharmacology; Phosphorus Isotopes; Proteins; Rats; Research; RNA; Tryptophan | 1964 |
INDUCTION OF HEME-PROTEIN ENZYME IN ANIMAL. 3. INDUCED SYNTHESIS OF APO-TRYPTOPHAN PEROXIDASE MOLECULE AND PROTOHEMIN IX.
Topics: Animals; Chromatography; Glycine; Heme; Hemeproteins; Hemin; Liver; Peroxidase; Peroxidases; Porphyrins; Proteins; Pyridines; Rats; Research; Spectrum Analysis; Tryptophan | 1964 |
STUDIES ON THE ROLE OF HEMATIN IN THE CATALYTIC MECHANISM OF TRYPTOPHAN PYRROLASE.
Topics: Catalysis; Coenzymes; Heme; Hemin; Kynurenine; Peroxidases; Porphyrins; Pseudomonas; Research; Spectrophotometry; Tryptophan; Tryptophan Oxygenase | 1965 |
EFFECTS OF PEROXIDE, CATALASE, AND HEMATIN IN THE ASSAY OF LIVER TRYPTOPHAN PYRROLASE.
Topics: Animals; Biochemical Phenomena; Biochemistry; Biological Assay; Catalase; Heme; Hemin; Hydrogen Peroxide; Kynurenine; Liver; Mice; Oxygenases; Peroxides; Pharmacology; Rats; Research; Spectrophotometry; Tryptophan; Tryptophan Oxygenase | 1965 |
Dynamic features of a heme delivery system for cytochrome C maturation.
Topics: Alanine; Amino Acid Motifs; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cell Division; Cytochromes c; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Hemeproteins; Histidine; Membrane Proteins; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Periplasm; Phenotype; Plasmids; Precipitin Tests; Protein Binding; Subcellular Fractions; Tryptophan | 2003 |
Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site.
Topics: Anisotropy; Bacterial Proteins; Binding Sites; Cold Temperature; Cyanobacteria; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Models, Molecular; Mutagenesis, Site-Directed; Peroxidases; Protein Conformation; Tryptophan | 2003 |
Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins.
Topics: Amino Acid Substitution; Animals; Aplysia; Apoproteins; Evolution, Molecular; Globins; Heme; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Tyrosine; Urea; Whales | 2004 |
Phe393 mutants of cytochrome P450 BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations.
Topics: Amino Acid Substitution; Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Ferric Compounds; Ferrous Compounds; Heme; Iron-Sulfur Proteins; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Phenylalanine; Propionates; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Substrate Specificity; Tryptophan; Tyrosine; Vinyl Compounds | 2004 |
Heme as an optical probe of a conformational transition of ovine recPrP.
Topics: Animals; Carbon Monoxide; Fluorescent Dyes; Heme; Peptides; Prions; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sheep; Spectrometry, Fluorescence; Temperature; Tryptophan; Tyrosine | 2004 |
Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intra-dimer coupling.
Topics: Absorption; Allosteric Regulation; Amino Acid Substitution; Carboxyhemoglobin; Dimerization; Escherichia coli; Genetic Variation; Heme; Hemoglobin A; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Oxygen; Photolysis; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Reference Standards; Reproducibility of Results; Spectrum Analysis, Raman; Tryptophan | 2004 |
Crystal structure of Mycobacterium tuberculosis catalase-peroxidase.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Heme; Models, Molecular; Molecular Sequence Data; Mutation; Mycobacterium tuberculosis; Peroxidases; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Tryptophan; Tyrosine | 2004 |
Optimised expression and purification of recombinant human indoleamine 2,3-dioxygenase.
Topics: Aminolevulinic Acid; Biochemistry; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Iron; Isopropyl Thiogalactoside; Kynurenine; Plasmids; Protoporphyrins; Recombinant Proteins; Temperature; Time Factors; Tryptophan; Tryptophan Oxygenase | 2004 |
Modulation of the folding energy landscape of cytochrome C with salt.
Topics: Cytochromes c; Fluorescence; Heme; Kinetics; Potassium Chloride; Protein Folding; Thermodynamics; Tryptophan | 2004 |
Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.
Topics: Bacillus subtilis; Bacterial Proteins; Biophysics; Carbon Monoxide; Circular Dichroism; Heme; Hydrogen-Ion Concentration; Kinetics; Leucine; Ligands; Models, Molecular; Mutation; Oxygen; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Signal Transduction; Spectrophotometry; Spectrophotometry, Infrared; Spectroscopy, Fourier Transform Infrared; Temperature; Time Factors; Tryptophan; Tyrosine; Ultracentrifugation; Ultraviolet Rays | 2005 |
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
Topics: Amino Acid Sequence; Apoproteins; Circular Dichroism; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Thermodynamics; Tryptophan; Urea | 2005 |
Monooxygenation of an aromatic ring by F43W/H64D/V68I myoglobin mutant and hydrogen peroxide. Myoglobin mutants as a model for P450 hydroxylation chemistry.
Topics: 5-Hydroxytryptophan; Animals; Binding Sites; Catalase; Catalysis; Chromatography, High Pressure Liquid; Chymotrypsin; Cytochrome P-450 Enzyme System; Escherichia coli; Heme; Hemeproteins; Hydrogen Peroxide; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Biological; Models, Chemical; Models, Molecular; Mutation; Myoglobin; Oxygen; Peptides; Phosphates; Potassium Compounds; Protein Structure, Tertiary; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry; Tryptophan; Ultraviolet Rays; Whales | 2005 |
A tryptophan that modulates tetrahydrobiopterin-dependent electron transfer in nitric oxide synthase regulates enzyme catalysis by additional mechanisms.
Topics: Animals; Arginine; Biopterins; Catalysis; Dimerization; Electron Transport; Enzyme Stability; Ferrous Compounds; Heme; Hydroxylation; Isoenzymes; Kinetics; Mice; Mutagenesis, Site-Directed; NADP; Nerve Tissue Proteins; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Binding; Rats; Spectrophotometry; Tryptophan | 2005 |
The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalase; Catalysis; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Methionine; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; Peptides; Peracetic Acid; Plasmids; Protein Binding; Recombinant Proteins; Spectrophotometry; Time Factors; Trypsin; Tryptophan; Tyrosine; Ultraviolet Rays | 2005 |
A biophysical investigation of recombinant hemoglobins with aromatic B10 mutations in the distal heme pockets.
Topics: Adult; Amino Acid Substitution; Azides; Heme; Hemoglobin A; Hemoglobins; Humans; Leucine; Nitric Oxide; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Phenylalanine; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Thermodynamics; Tryptophan | 2005 |
Characterization of the oxidase activity in mammalian catalase.
Topics: Animals; Benzidines; Blotting, Western; Catalase; Catechin; Cattle; Cell Line; Coumaric Acids; Cricetinae; Heme; Humans; Hydrogen Peroxide; Indoles; Iron; Kinetics; Laccase; Mice; Mitochondria; Models, Biological; Models, Chemical; Models, Molecular; Oxidoreductases; Oxygen; Peroxidases; Phenethylamines; Protein Binding; Protein Conformation; Spectrophotometry; Temperature; Time Factors; Tryptophan; Vanillic Acid | 2005 |
Proximal effects in the modulation of nitric oxide synthase reactivity: a QM-MM study.
Topics: Binding Sites; Computational Biology; Heme; Hemeproteins; Humans; Hydrogen Bonding; Iron; Models, Molecular; Nitric Oxide Synthase Type III; Tryptophan | 2005 |
Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450.
Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Iron; Protein Structure, Tertiary; Tryptophan; Tyrosine | 2005 |
Picosecond structural dynamics of myoglobin following photodissociation of carbon monoxide as revealed by ultraviolet time-resolved resonance Raman spectroscopy.
Topics: Carbon Monoxide; Heme; Models, Molecular; Myoglobin; Photolysis; Spectrum Analysis, Raman; Time Factors; Tryptophan; Tyrosine; Ultraviolet Rays | 2005 |
Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis.
Topics: Bacterial Proteins; Electrochemistry; Heme; Indolequinones; Kinetics; Models, Molecular; Oxidation-Reduction; Oxygen; Paracoccus denitrificans; Tryptophan | 2006 |
Evidence for displacements of the C-helix by CO ligation and DNA binding to CooA revealed by UV resonance Raman spectroscopy.
Topics: Bacterial Proteins; Carbon Monoxide; DNA; Electrons; Heme; Hemeproteins; Iron; Kinetics; Ligands; Models, Molecular; Molecular Conformation; Protein Binding; Protein Conformation; Protein Structure, Secondary; Rhodospirillum rubrum; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Time Factors; Trans-Activators; Tryptophan; Ultraviolet Rays | 2006 |
Interactions between nitric oxide and indoleamine 2,3-dioxygenase.
Topics: Heme; Humans; Hydrogen-Ion Concentration; Indoleamine-Pyrrole 2,3,-Dioxygenase; Iron; Nitric Oxide; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Spectrum Analysis, Raman; Tryptophan | 2006 |
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.
Topics: Binding Sites; Crystallography, X-Ray; Glycine; Heme; Indoleamine-Pyrrole 2,3,-Dioxygenase; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Folding; Quinolinic Acid; Ralstonia; Structure-Activity Relationship; Substrate Specificity; Tryptophan; Tryptophan Oxygenase | 2007 |
Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase.
Topics: Ascorbate Peroxidases; Bacterial Proteins; Catalase; Chromatography, High Pressure Liquid; Cytochrome-c Peroxidase; Deuteroporphyrins; Glycine max; Heme; Hydrogen Peroxide; Oxidation-Reduction; Peroxidases; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis; Tandem Mass Spectrometry; Tryptophan | 2007 |
NikA binds heme: a new role for an Escherichia coli periplasmic nickel-binding protein.
Topics: ATP-Binding Cassette Transporters; Escherichia coli Proteins; Heme; Models, Molecular; Nickel; Periplasm; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 2007 |
Irreversible cross-linking of heme to the distal tryptophan of stromal ascorbate peroxidase in response to rapid inactivation by H2O2.
Topics: Amino Acid Sequence; Apoproteins; Ascorbate Peroxidases; Binding Sites; Catalytic Domain; Chloroplasts; Cross-Linking Reagents; Heme; Hydrogen Peroxide; Models, Molecular; Molecular Sequence Data; Mutation; Nicotiana; Peroxidases; Plant Proteins; Protein Binding; Recombinant Proteins; Tryptophan | 2007 |
PGH2 degradation pathway catalyzed by GSH-heme complex bound microsomal prostaglandin E2 synthase type 2: the first example of a dual-function enzyme.
Topics: Binding Sites; Catalysis; Color; Crystallography, X-Ray; Glutathione; Heme; Humans; Intramolecular Oxidoreductases; Lipocalins; Microsomes; Models, Molecular; Prostaglandin H2; Prostaglandin-E Synthases; Protein Folding; Tryptophan | 2007 |
Kinetic resolution of a tryptophan-radical intermediate in the reaction cycle of Paracoccus denitrificans cytochrome c oxidase.
Topics: Computer Simulation; Copper; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Freezing; Heme; Kinetics; Oxidation-Reduction; Paracoccus denitrificans; Spectrophotometry, Ultraviolet; Tryptophan | 2007 |
The roles of Tyr(CD1) and Trp(G8) in Mycobacterium tuberculosis truncated hemoglobin O in ligand binding and on the heme distal site architecture.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; DNA Primers; Heme; Hemoglobins; Hydrogen Bonding; Ligands; Mutagenesis; Spectrum Analysis, Raman; Truncated Hemoglobins; Tryptophan; Tyrosine | 2007 |
The reactivity of heme in biological systems: autocatalytic formation of both tyrosine-heme and tryptophan-heme covalent links in a single protein architecture.
Topics: Amino Acid Sequence; Ascorbate Peroxidases; Catalysis; Chromatography, High Pressure Liquid; Electron Spin Resonance Spectroscopy; Glycine max; Heme; Hydrogen Peroxide; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peroxidases; Recombinant Proteins; Tryptophan; Tyrosine | 2007 |
The hierarchy of structural transitions induced in cytochrome c by anionic phospholipids determines its peroxidase activation and selective peroxidation during apoptosis in cells.
Topics: Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Activation; Etoposide; Fluorescence; Heme; Humans; Mice; Peroxidase; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositol Phosphates; Phosphatidylserines; Phospholipids; Protein Structure, Tertiary; Tryptophan | 2007 |
Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase.
Topics: Binding Sites; Crystallography, X-Ray; Enzyme Activation; Heme; Hydrogen-Ion Concentration; Iron; Isoleucine; Kinetics; Models, Molecular; Mutation; Oxidation-Reduction; Oxygen; Oxygenases; Phenol; Protein Structure, Tertiary; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis; Substrate Specificity; Tryptophan | 2007 |
Phospholipid membranes affect tertiary structure of the soluble cytochrome b5 heme-binding domain.
Topics: Calorimetry; Chromatography, Gel; Circular Dichroism; Cytochromes b5; Fluorescence; Heme; Magnetic Resonance Spectroscopy; Phospholipids; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Solubility; Temperature; Tryptophan; Unilamellar Liposomes | 2008 |
A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
Topics: Bacterial Proteins; Catalysis; Free Radicals; Heme; Hemeproteins; Indolequinones; Iron; Paracoccus denitrificans; Protein Processing, Post-Translational; Spectroscopy, Mossbauer; Tryptophan | 2008 |
Ultrafast proteinquake dynamics in cytochrome c.
Topics: Animals; Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photolysis; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan | 2009 |
Peroxide-dependent formation of a covalent link between Trp51 and the heme in cytochrome c peroxidase.
Topics: Chromatography, High Pressure Liquid; Cytochrome-c Peroxidase; Heme; Molecular Structure; Oxidants; Peroxides; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tryptophan | 2009 |
Reassessment of the reaction mechanism in the heme dioxygenases.
Topics: Catalysis; Chemistry, Organic; Dioxygenases; Heme; Indoleamine-Pyrrole 2,3,-Dioxygenase; Indoles; Kinetics; Kynurenine; Models, Chemical; Mutagenesis, Site-Directed; Oxygen; Protons; Tryptophan; Tryptophan Oxygenase | 2009 |
Trp180 of endothelial NOS and Trp56 of bacterial saNOS modulate sigma bonding of the axial cysteine to the heme.
Topics: Animals; Cloning, Molecular; Cysteine; Endothelium; Heme; Hydrogen Bonding; Mutation; Nitric Oxide; Nitric Oxide Synthase Type III; Spectrum Analysis, Raman; Staphylococcus aureus; Tryptophan | 2009 |
Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals.
Topics: Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Lipid Peroxidation; Nitrosation; Oxidation-Reduction; Oxidative Stress; Peroxidase; Peroxynitrous Acid; Protein Processing, Post-Translational; Protein Structure, Secondary; Spectrophotometry; Superoxides; Tryptophan; Unilamellar Liposomes | 2009 |
Structure and catalytic behavior of myoglobin adsorbed onto nanosized hydrotalcites.
Topics: Adsorption; Aluminum; Aluminum Hydroxide; Animals; Biocatalysis; Guaiacol; Heme; Horses; Hydrogen Peroxide; Hydrogen-Ion Concentration; Immobilized Proteins; Iron; Kinetics; Magnesium Hydroxide; Models, Chemical; Models, Molecular; Myoglobin; Nanoparticles; Nickel; Oxidation-Reduction; Peroxidase; Porphyrins; Protein Conformation; Spectrum Analysis; Tryptophan | 2009 |
Ligand and substrate migration in human indoleamine 2,3-dioxygenase.
Topics: Binding Sites; Carbon Monoxide; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Ligands; Photolysis; Protein Conformation; Recombinant Proteins; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Tryptophan | 2009 |
Ultrafast dynamics of resonance energy transfer in myoglobin: probing local conformation fluctuations.
Topics: Animals; Energy Transfer; Heme; Kinetics; Molecular Dynamics Simulation; Movement; Mutation; Myoglobin; Protein Engineering; Protein Structure, Secondary; Quantum Theory; Spectrometry, Fluorescence; Temperature; Tryptophan | 2010 |
The ternary complex of PrnB (the second enzyme in the pyrrolnitrin biosynthesis pathway), tryptophan, and cyanide yields new mechanistic insights into the indolamine dioxygenase superfamily.
Topics: Amino Acid Transport Systems, Neutral; Binding Sites; Calorimetry; Cyanides; DNA Primers; Emericella; Fungal Proteins; Heme; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Tryptophan; Tryptophan Oxygenase | 2010 |
Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.
Topics: Catalysis; Electron Transport; Electrons; Heme; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Protein Processing, Post-Translational; Tryptophan | 2010 |
A specific interaction of L-tryptophan with CO of CO-bound indoleamine 2,3-dioxygenase identified by resonance Raman spectroscopy.
Topics: Carbon Monoxide; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Iron; Spectrum Analysis, Raman; Stereoisomerism; Tryptophan | 2010 |
Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Biocatalysis; Carbon Monoxide; Crystallography, X-Ray; Cytochrome-c Peroxidase; Ferrous Compounds; Glutamic Acid; Heme; Hemeproteins; Indolequinones; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nitric Oxide; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity; Tryptophan | 2011 |
Characterization of heme-binding properties of Paracoccus denitrificans Surf1 proteins.
Topics: Cloning, Molecular; Electron Transport Complex IV; Escherichia coli; Heme; Membrane Proteins; Mitochondrial Proteins; Models, Chemical; Paracoccus denitrificans; Tryptophan | 2011 |
Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni.
Topics: Bacterial Proteins; Campylobacter jejuni; Glycine; Heme; Histidine; Hydrogen Bonding; Ligands; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Oxygen; Protein Binding; Spectrum Analysis, Raman; Truncated Hemoglobins; Tryptophan; Tyrosine | 2011 |
Ultrafast dynamics of nonequilibrium resonance energy transfer and probing globular protein flexibility of myoglobin.
Topics: Fluorescence Resonance Energy Transfer; Heme; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Myoglobin; Pliability; Protein Structure, Secondary; Recombinant Proteins; Solutions; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Tryptophan | 2012 |
Femtosecond UV studies of the electronic relaxation processes in Cytochrome c.
Topics: Animals; Cytochromes c; Electrons; Energy Transfer; Heme; Horses; Oxidation-Reduction; Spectrophotometry, Ultraviolet; Time Factors; Tryptophan | 2011 |
Extracellular heme enhances the antimalarial activity of artemisinin.
Topics: Antimalarials; Antioxidants; Artemisia; Artemisinins; Chloroquine; Cholesterol, LDL; Fluorescence; Heme; Hemin; Humans; Lipid Peroxidation; Mefloquine; Oxidants; Oxidation-Reduction; Plasmodium falciparum; Quinine; Tryptophan; Vitamin E | 2012 |
The mechanism of substrate inhibition in human indoleamine 2,3-dioxygenase.
Topics: Biochemistry; Catalysis; Chemistry, Pharmaceutical; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kinetics; Kynurenine; Mutagenesis, Site-Directed; Oxygen; Protein Binding; Substrate Specificity; Thermodynamics; Tryptophan | 2012 |
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.
Topics: Bacterial Proteins; Catalysis; Crystallography, X-Ray; Heme; Hemeproteins; Indolequinones; Kinetics; Ligands; Mass Spectrometry; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Proline; Tryptophan | 2012 |
PpsR, a regulator of heme and bacteriochlorophyll biosynthesis, is a heme-sensing protein.
Topics: Bacteriochlorophylls; Deoxyribonuclease I; DNA; DNA-Binding Proteins; Escherichia coli; Gene Expression Regulation; Heme; Iron; Ligands; Molecular Conformation; Photosynthesis; Protein Binding; Protein Structure, Tertiary; Proteobacteria; Rhodobacter sphaeroides; Tetrapyrroles; Tryptophan | 2012 |
Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase.
Topics: Base Sequence; Catalysis; Coloring Agents; Crystallography, X-Ray; Escherichia coli; Heme; Kinetics; Models, Chemical; Molecular Conformation; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Peroxidases; Phenol; Pleurotus; Proteins; Spectrophotometry; Tryptophan | 2012 |
Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.
Topics: Bacterial Proteins; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Indolequinones; Ligands; Lysine; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Peroxides; Protein Processing, Post-Translational; Spectrophotometry; Tryptophan; Tyrosine | 2012 |
Understanding the roles of strictly conserved tryptophan residues in O2 producing chlorite dismutases.
Topics: Biocatalysis; Chlorides; Conserved Sequence; Enzyme Stability; Heme; Kinetics; Ligands; Models, Molecular; Mutation; Oxidoreductases; Oxygen; Peracetic Acid; Protein Conformation; Rhodocyclaceae; Spectrum Analysis; Thermodynamics; Tryptophan | 2013 |
Probing ligand binding to thromboxane synthase.
Topics: Amino Acid Sequence; Binding Sites; Catalysis; Computer Simulation; Cytochrome P-450 CYP3A; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Heme; Humans; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutation; Naphthalenesulfonates; Oxazines; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrometry, Fluorescence; Thromboxane-A Synthase; Tryptophan | 2013 |
Ultrafast tryptophan-to-heme electron transfer in myoglobins revealed by UV 2D spectroscopy.
Topics: Animals; Electron Transport; Fluorescence Resonance Energy Transfer; Heme; Horses; Myoglobin; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Tryptophan | 2013 |
Detection and analysis of protofibrils and fibrils of hemoglobin: implications for the pathogenesis and cure of heme loss related maladies.
Topics: Absorption; Acrylamide; Anilino Naphthalenesulfonates; Animals; Cattle; Dose-Response Relationship, Drug; Hematologic Diseases; Heme; Hemoglobins; Protein Multimerization; Spectrometry, Fluorescence; Trifluoroethanol; Tryptophan | 2013 |
Chemistry. FRETting over the spectroscopic ruler.
Topics: Animals; Heme; Myoglobin; Spectrophotometry, Ultraviolet; Tryptophan | 2013 |
Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.
Topics: Catalysis; Enzyme Precursors; Ferric Compounds; Heme; Hemeproteins; Histidine; Indolequinones; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Processing, Post-Translational; Spectroscopy, Near-Infrared; Tryptophan; Tyrosine | 2013 |
Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.
Topics: Crystallography, X-Ray; Ferric Compounds; Ferrous Compounds; Glutamic Acid; Heme; Hemeproteins; Hydrogen Peroxide; Indolequinones; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan | 2013 |
The kinetics of the reaction of nitrogen dioxide with iron(II)- and iron(III) cytochrome c.
Topics: Amino Acids; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Nitrogen Dioxide; Oxidation-Reduction; Pulse Radiolysis; Tryptophan; Tyrosine | 2014 |
Differential roles of tryptophan residues in conformational stability of Porphyromonas gingivalis HmuY hemophore.
Topics: Amino Acid Substitution; Bacterial Proteins; Heme; Porphyromonas gingivalis; Protein Binding; Protein Stability; Protein Structure, Tertiary; Protein Unfolding; Temperature; Tryptophan | 2014 |
Identifying the elusive sites of tyrosyl radicals in cytochrome c peroxidase: implications for oxidation of substrates bound at a site remote from the heme.
Topics: Amino Acid Substitution; Binding Sites; Biocatalysis; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Electron Transport; Expectorants; Guaiacol; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Oxidation-Reduction; Protein Conformation; Recombinant Fusion Proteins; Saccharomyces cerevisiae Proteins; Surface Properties; Tryptophan; Tyrosine | 2014 |
Naturally-occurring tetrahydro-β-carboline alkaloids derived from tryptophan are oxidized to bioactive β-carboline alkaloids by heme peroxidases.
Topics: Ascorbic Acid; Carbolines; Enzyme Inhibitors; Harmine; Heme; Horseradish Peroxidase; Hydroxylamine; Kinetics; Lactoperoxidase; Oxidation-Reduction; Peroxidase; Peroxidases; Sodium Azide; Tryptophan | 2014 |
Structural and functional analyses of human tryptophan 2,3-dioxygenase.
Topics: Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Heme; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Sequence Homology, Amino Acid; Tryptophan; Tryptophan Oxygenase | 2014 |
Computational insight into nitration of human myoglobin.
Topics: Catalytic Domain; Heme; Humans; Molecular Dynamics Simulation; Myoglobin; Nitrites; Protein Conformation; Protein Processing, Post-Translational; Tryptophan; Tyrosine | 2014 |
Heme-binding-mediated negative regulation of the tryptophan metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1) by IDO2.
Topics: Cell Proliferation; Cell Survival; Gene Expression; HEK293 Cells; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Protein Binding; Tryptophan; Up-Regulation | 2014 |
Inhibitory effects of deferasirox on the structure and function of bovine liver catalase: a spectroscopic and theoretical study.
Topics: Animals; Benzoates; Binding, Competitive; Catalase; Catalytic Domain; Cattle; Circular Dichroism; Deferasirox; Enzyme Inhibitors; Heme; Hydrophobic and Hydrophilic Interactions; Iron; Iron Chelating Agents; Kinetics; Liver; Molecular Docking Simulation; Protein Binding; Protein Structure, Secondary; Solutions; Spectrometry, Fluorescence; Temperature; Thermodynamics; Triazoles; Tryptophan | 2015 |
Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.
Topics: Amino Acid Substitution; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Indolequinones; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Spectroscopy, Near-Infrared; Temperature; Tryptophan | 2015 |
A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.
Topics: Bacterial Proteins; Crystallography, X-Ray; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Hemeproteins; Indolequinones; Models, Molecular; Mutation; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tryptophan | 2015 |
Tryptophan-to-heme electron transfer in ferrous myoglobins.
Topics: Algorithms; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Kinetics; Leucine; Models, Chemical; Models, Molecular; Myoglobin; Porphyrins; Protein Structure, Tertiary; Spectrophotometry; Tryptophan; Valine | 2015 |
Initial O₂ Insertion Step of the Tryptophan Dioxygenase Reaction Proposed by a Heme-Modification Study.
Topics: Acetylation; Animals; Bacterial Proteins; Biocatalysis; Camphor 5-Monooxygenase; Carbon Dioxide; Delftia acidovorans; Deuteroporphyrins; Heme; Kynurenine; Ligands; Mesoporphyrins; Models, Molecular; Myoglobin; Oxidation-Reduction; Oxygen; Tryptophan; Tryptophan Oxygenase | 2015 |
Density Functional Theory Insights into the Role of the Methionine-Tyrosine-Tryptophan Adduct Radical in the KatG Catalase Reaction: O2 Release from the Oxyheme Intermediate.
Topics: Bacterial Proteins; Carbon; Catalase; Catalysis; Electrons; Heme; Hydrogen; Hydrogen Bonding; Methionine; Models, Chemical; Mycobacterium tuberculosis; Nitrogen; Oxygen; Quantum Theory; Tryptophan; Tyrosine | 2015 |
Is tryptophan metabolism involved in sleep apnea-related cardiovascular co-morbidities and cancer progression?
Topics: Adult; Animals; Cardiovascular Diseases; Comorbidity; Disease Progression; Heme; Humans; Hypoxia; Mice; Models, Theoretical; Neoplasms; Obesity; Rats; Risk Factors; Sleep Apnea, Obstructive; Tryptophan | 2015 |
Discovery of a regioselectivity switch in nitrating P450s guided by molecular dynamics simulations and Markov models.
Topics: Catalysis; Catalytic Domain; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Heme; Histidine; Markov Chains; Molecular Dynamics Simulation; Mutagenesis; Protein Conformation; Stereoisomerism; Streptomyces; Tryptophan | 2016 |
Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid Derivatives Is Dependent on Peroxide Tone.
Topics: Amino Acid Substitution; Binding Sites; Crystallography, X-Ray; Cyclooxygenase 2; Cyclooxygenase 2 Inhibitors; Endocannabinoids; Fenamates; Heme; Humans; In Vitro Techniques; Models, Molecular; Mutagenesis, Site-Directed; Peroxides; Recombinant Proteins; Substrate Specificity; Tryptophan | 2016 |
High l-Trp affinity of indoleamine 2,3-dioxygenase 1 is attributed to two residues located in the distal heme pocket.
Topics: Amino Acids; Animals; Catalytic Domain; Evolution, Molecular; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Sequence Alignment; Sequence Analysis, Protein; Tryptophan; Tryptophan Oxygenase | 2016 |
Quantum chemical calculations of tryptophan → heme electron and excitation energy transfer rates in myoglobin.
Topics: Density Functional Theory; Electrons; Energy Transfer; Heme; Hydrogen Bonding; Isoleucine; Microscopy; Myoglobin; Protein Conformation; Spectrophotometry, Ultraviolet; Tryptophan; Valine | 2017 |
Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.
Topics: Antioxidants; Ascorbate Peroxidases; Ascorbic Acid; Bacterial Proteins; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Hydroxyurea; Indolequinones; Iron; Kinetics; Mutant Proteins; Oxidation-Reduction; Oxidative Stress; Paracoccus denitrificans; Spectrum Analysis; Time Factors; Tryptophan | 2017 |
Hole Hopping through Tryptophan in Cytochrome P450.
Topics: Archaeal Proteins; Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Electron Transport; Heme; Models, Molecular; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Photosensitizing Agents; Ruthenium; Sulfolobus acidocaldarius; Tryptophan | 2017 |
Theory Uncovers the Role of the Methionine-Tyrosine-Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O
Topics: Catalase; Catalytic Domain; Electron Transport; Free Radicals; Heme; Histidine; Methionine; Molecular Dynamics Simulation; Oxidation-Reduction; Oxygen; Peroxidases; Protein Conformation; Protons; Tryptophan; Tyrosine | 2018 |
Vibrational Energy Transfer from Heme through Atomic Contacts in Proteins.
Topics: Animals; Energy Transfer; Heme; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Myoglobin; Recombinant Proteins; Spectrum Analysis, Raman; Tryptophan; Whales | 2018 |
Living with Oxygen.
Topics: Catalytic Domain; Coordination Complexes; Cysteine; Cytochrome P-450 Enzyme System; Heme; Metals, Heavy; Methionine; Oxidation-Reduction; Oxygen; Protein Structural Elements; Tryptophan; Tyrosine | 2018 |
High-resolution structures of inhibitor complexes of human indoleamine 2,3-dioxygenase 1 in a new crystal form.
Topics: Catalytic Domain; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Mutation; Tryptophan; Urea | 2018 |
UV Resonance Raman Characterization of a Substrate Bound to Human Indoleamine 2,3-Dioxygenase 1.
Topics: Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Oxygen; Protein Binding; Protein Conformation; Spectrum Analysis, Raman; Tryptophan | 2019 |
Electron transfer pathways from quantum dynamics simulations.
Topics: Electron Transport; Heme; Models, Chemical; Molecular Dynamics Simulation; Peroxidases; Phenylalanine; Quantum Theory; Trypanosoma cruzi; Tryptophan | 2020 |
Multiple roles of haem in cystathionine β-synthase activity: implications for hemin and other therapies of acute hepatic porphyria.
Topics: Animals; Cystathionine beta-Synthase; Heme; Hemin; Homocysteine; Humans; Kynurenine; Nutritional Status; Porphyrias, Hepatic; Treatment Outcome; Tryptophan; Vitamin B Complex | 2021 |
Indoleamine dioxygenase and tryptophan dioxygenase activities are regulated through GAPDH- and Hsp90-dependent control of their heme levels.
Topics: Enzyme Inhibitors; HEK293 Cells; HeLa Cells; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Tryptophan; Tryptophan Oxygenase | 2022 |
Computational analysis of the tryptophan cation radical energetics in peroxidase Compound I.
Topics: Cations; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Hydrogen Peroxide; Oxidation-Reduction; Peroxidase; Peroxidases; Tryptophan | 2022 |
Dependence of Vibrational Energy Transfer on Distance in a Four-Helix Bundle Protein: Equidistant Increments with the Periodicity of α Helices.
Topics: Energy Transfer; Heme; Protein Conformation, alpha-Helical; Tryptophan; Vibration | 2022 |
Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.
Topics: Heme; Hydrogen Peroxide; Oxidation-Reduction; Oxidoreductases; Oxygen; Tryptophan; Tyrosine; Water | 2023 |
Tryptophan-96 in cytochrome P450 BM3 plays a key role in enzyme survival.
Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Heme; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Tryptophan; Tyrosine | 2023 |
Pyridine-containing substrate analogs are restricted from accessing the human cytochrome P450 8B1 active site by tryptophan 281.
Topics: Catalytic Domain; Cytochrome P-450 Enzyme System; Diabetes Mellitus, Type 2; Heme; Humans; Iron; Pyridines; Steroid 12-alpha-Hydroxylase; Steroids; Tryptophan | 2023 |
Ultrafast Energy Transfer from Photoexcited Tryptophan to the Haem in Cytochrome c.
Topics: Cytochromes c; Electron Transport; Energy Transfer; Heme; Iron; Tryptophan | 2023 |
Indoleamine dioxygenase and tryptophan dioxygenase activities are regulated through control of cell heme allocation by nitric oxide.
Topics: Animals; Heme; Indoleamine-Pyrrole 2,3,-Dioxygenase; Mammals; Nitric Oxide; Tryptophan; Tryptophan Oxygenase | 2023 |
Hydroxytryptophan biosynthesis by a family of heme-dependent enzymes in bacteria.
Topics: 5-Hydroxytryptophan; Animals; Bacteria; Heme; Humans; Melatonin; Tryptophan | 2023 |
Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation.
Topics: Antioxidants; Glutathione; Heme; Hemoglobins; Humans; Oxygen; Oxyhemoglobins; Tryptophan | 2023 |