histidine has been researched along with carbon monoxide in 173 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 44 (25.43) | 18.7374 |
| 1990's | 45 (26.01) | 18.2507 |
| 2000's | 58 (33.53) | 29.6817 |
| 2010's | 24 (13.87) | 24.3611 |
| 2020's | 2 (1.16) | 2.80 |
| Authors | Studies |
|---|---|
| Amiconi, G; Antonini, E; Bonaventura, C; Bonaventura, J; Brunori, M; Tentori, L | 2 |
| Richards, JH; Satterlee, JD; Teintze, M | 1 |
| Galacteros, F; Kister, J; Lahary, A; Marden, M; Monconduit, M; Wajcman, H | 1 |
| Kraut, J; Miller, MA; Smulevich, G; Spiro, TG | 1 |
| Bonaventura, C; Bonaventura, J; Cashon, R; Fermi, G; Perutz, M; Shih, DT | 1 |
| Champion, PM; Srajer, V | 1 |
| Blackmore, RS; Carver, TE; Gibson, QH; Olson, JS; Rohlfs, RJ; Sligar, SG; Springer, BA | 1 |
| Ramsden, J; Spiro, TG | 1 |
| Adachi, S; Morishima, I; Orii, Y; Shiro, Y; Yano, Y | 1 |
| Egeberg, KD; Mathews, AJ; Olson, JS; Rohlfs, RJ; Sligar, SG; Springer, BA | 1 |
| English, AM; Fishel, LA; Kraut, J; Mauro, JM; Smulevich, G; Spiro, TG | 1 |
| Behere, DV; Goff, HM; Gonzalez-Vergara, E | 1 |
| Egeberg, KD; Mathews, AJ; Nagai, K; Olson, JS; Renaud, JP; Rohlfs, RJ; Sligar, SG; Springer, BA; Tame, J | 1 |
| Ansari, A; Berendzen, J; Braunstein, D; Cowen, BR; Egeberg, KD; Frauenfelder, H; Hong, MK; Ormos, P; Sauke, TB; Scholl, R | 1 |
| Dalvit, C; Tennant, L; Wright, PE | 1 |
| Ascenzi, P; Brunori, M; Coletta, M; Traylor, TG | 1 |
| Bartnicki, DE; Kerr, EA; Mizukami, H; Yu, NT | 1 |
| Caughey, WS | 1 |
| Momenteau, M | 1 |
| Friedrich, W; Moskophidis, M; Pohl, CM | 1 |
| Huestis, WH; Raftery, MA | 1 |
| Gibson, QH; Hamilton, HB; Nagel, RL; Olson, JS | 1 |
| Ho, C; Lindstrom, TR | 1 |
| Gibson, QH; Hewitt, JA | 1 |
| Gibson, QH; Kilmartin, JV; Moffat, K; Olson, JS | 1 |
| Pulsinelli, PD | 1 |
| Bonaventura, C; Bonaventura, J; Sullivan, B | 1 |
| Gibson, QH; Olson, JS | 1 |
| Brown, WD; Duffy, P; Wu, CS | 1 |
| Geraci, G; Sada, A | 1 |
| Maruyama, K; Yagi, T | 1 |
| de Bruin, SH; Janssen, LH; van Os, GA | 1 |
| Reed, T | 1 |
| Amiconi, G; Anderson, NM; Antonini, E; Brunori, M; Winterhalter, KH | 1 |
| Caughey, W; McCoy, S | 1 |
| Briehl, RW; Hobbs, JF | 1 |
| Jacob, HS; Winterhalter, KH | 1 |
| Geraci, G; Gibson, QH; Parkhurst, LJ | 1 |
| Bucci, E; Fronticelli, C; Ragatz, B | 1 |
| Ellerton, HD; Ellerton, NF; Robinson, HA | 1 |
| Heger, M; Mohtashamipur, E; Norpoth, K | 1 |
| DiIorio, EE; Dlott, DD; Frauenfelder, H; Langer, P; Roder, H | 1 |
| Kwiatkowski, LD; Noble, RW | 1 |
| John, ME; Sharma, VS; Waterman, MR | 1 |
| Kajita, A; Ohe, M | 1 |
| Krümpelmann, D; Ribbing, W; Rüterjans, H | 1 |
| Ribbing, W; Rüterjans, H | 2 |
| Gibson, QH; Lai, HH; Li, T; Lyons, DS; Olson, JS; Phillips, GN | 1 |
| Anderton, CL; Hester, RE; Moore, JN | 1 |
| Meunier, B; Rich, PR; Rodriguez-Lopez, JN; Smith, AT; Thorneley, RN | 1 |
| Admiraal, SJ; Dou, Y; George, GN; Ikeda-Saito, M; Krzywda, S; Li, T; Olson, JS; Pickering, IJ; Prince, RC; Wilkinson, AJ | 1 |
| Kempf, AC; Meyer, UA; Zanger, UM | 1 |
| Jewsbury, P; Kitagawa, T | 1 |
| Burstyn, JN; Dawson, JH; Dierks, EA; Hawkins, BK; Yu, AE | 1 |
| Gregoriou, VG; Hu, X; Jayaraman, V; Spiro, TG | 1 |
| Dean, DR; Kim, CH; Newton, WE | 1 |
| Loehr, TM; Ortiz de Montellano, PR; Sun, J; Wilks, A | 1 |
| Balasubramanian, S; Boxer, SG; Iizuka, T; Kitagawa, T; Marubayashi, K; Ogura, T; Shiro, Y | 1 |
| Anraku, Y; Hori, H; Mogi, T; Nishimura, Y; Tsubaki, M; Uno, T | 1 |
| Li, T; Olson, JS; Phillips, GN; Quillin, ML | 1 |
| Imai, K; Ishimori, K; Konno, T; Miyazaki, G; Morishima, I; Togi, A; Unno, M | 1 |
| Boffi, A; Chiancone, E; Friedman, JM; Rousseau, DL; Song, S | 1 |
| Fraunfelter, FA; Ikeda-Saito, M; Kitagawa, T; Mattera, R; Ogura, T; Sakan, Y | 1 |
| Brunori, M; Cavalli, V; Vallone, B; Vecchini, P | 1 |
| Phillips, GN; Yang, F | 1 |
| Chance, MR; Fischetti, RF; Hai, Y; Huang, WX; Miller, LM; Scheuring, E; Sclavi, B; Sullivan, M | 1 |
| Blackburn, NJ; Boswell, JS; Kulathila, R; Merkler, D; Reedy, BJ | 1 |
| Adachi, S; Bourgeois, D; Moffat, K; Pradervand, C; Ren, Z; Schildkamp, W; Srajer, V; Teng, T; Ursby, T; Wulff, M | 1 |
| Kushkuley, B; Stavrov, SS | 1 |
| Arredondo-Peter, R; Barry, JK; Berry, MB; Brucker, EA; Dean, JM; Hargrove, MS; Klucas, RV; Olson, JS; Phillips, GN; Sarath, G | 1 |
| Buchter, S; Galkin, O; Schulte, A; Tabirian, A | 1 |
| Hori, H; Mogi, T; Tsubaki, M | 1 |
| Boffi, A; Chiancone, E; Colotti, G; Das, TK; Gibson, QH; Guarrera, L; Rousseau, DL | 1 |
| Chien, EY; La Mar, GN; Sligar, SG; Wu, Y | 1 |
| Marletta, MA; Stone, JR | 1 |
| Feis, A; Rodriguez-Lopez, JN; Smulevich, G; Thorneley, RN | 1 |
| Babcock, GT; Marletta, MA; Schelvis, JP; Zhao, Y | 1 |
| Lanzilotta, WN; Lemon, BJ; Peters, JW; Seefeldt, LC | 1 |
| Burstyn, JN; Chung, SY; Kerby, RL; Parks, RB; Reynolds, MF; Roberts, GP; Shelver, D; Thorsteinsson, MV | 1 |
| Bartunik, HD; Kachalova, GS; Popov, AN | 1 |
| Blackburn, NJ; Morgan, JE; Ralle, M; Verkhovskaya, ML; Verkhovsky, MI; Wikström, M | 1 |
| Arese, M; Bellelli, A; Brunori, M; Brzezinski, P; Cutruzzolà, F; Grasso, S; Liberti, S; Wilson, EK | 1 |
| Sagnella, DE; Straub, JE | 1 |
| Ryde, U; Sigfridsson, E | 1 |
| Berendzen, J; Chu, K; Schlichting, I; Sweet, RM; Vojtechovský, J | 1 |
| Blackburn, NJ; Jaron, S | 1 |
| Babcock, GT; Cerda, JF; Choi, CY; Chu, HA; Marletta, MA | 1 |
| Moënne-Loccoz, P; Wilks, A | 1 |
| Kerby, RL; Roberts, GP; Thorsteinsson, MV | 1 |
| Aono, S; Ishikawa, H; Ishimori, K; Kitagawa, T; Mizutani, Y; Morishima, I; Nakajima, H; Uchida, T | 1 |
| Iizuka, T; Mukai, M; Nakamura, H; Nakamura, K; Shiro, Y | 1 |
| Hori, H; Ishimori, K; Morishima, I; Takahashi, S; Yoshioka, S | 1 |
| Bhattacharya, S; Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC; Wang, Y | 1 |
| Bailey, J; Boxer, SG; Dyer, RB; Franzen, S; Hu, RB; Thomas, MR; Woodruff, WH | 1 |
| Eichinger, M; Evanseck, JD; Parrinello, M; Rovira, C; Schulze, B | 1 |
| Boxer, SG; Thomas, MR | 1 |
| Aerts, T; Baudin-Creuza, V; Burmester, T; Caubergs, R; Dewilde, S; Hankeln, T; Kiger, L; Marden, MC; Moens, L | 1 |
| Lynch, JW; Seebungkert, B | 1 |
| Benton, PM; Dean, DR; Hoffman, BM; Mayer, SM; Seefeldt, LC; Shao, J | 1 |
| Hirota, S; Kitagawa, T; Mizoguchi, Y; Yamauchi, O | 1 |
| Boffi, A; Draghi, F; Miele, AE; Vallone, B | 1 |
| Kitagawa, T; Mizutani, Y; Sagami, I; Sasakura, Y; Sato, A; Shimizu, T; Sugiyama, S | 1 |
| Dreuw, A; Dunietz, BD; Head-Gordon, M | 1 |
| Bhuyan, AK; Kumar, R | 1 |
| Blackburn, NJ; Eipper, BA; Jaron, S; Mains, RE | 1 |
| Hori, H; Ishikawa, H; Ishimori, K; Matts, RL; Morishima, I; Takahashi, S; Yun, BG | 1 |
| Bailey, JA; Donohoe, RJ; Dyer, RB; Gennis, RB; Li, Z; Martinez, RA; Silks, LA; Tomson, F; Unkefer, CJ; Woodruff, WH | 1 |
| Hargrove, MS; Kundu, S | 1 |
| Homma, N; Hori, H; Makino, R; Obayashi, E; Shiro, Y | 1 |
| Farmer, PJ; Fleischer, E; La Mar, GN; Ma, D; Sulc, F | 1 |
| Dalosto, SD; Kaposi, AD; Prabhu, NV; Sharp, KA; Stavrov, SS; Vanderkooi, JM; Wright, WW | 1 |
| Hayashi, T; Ishikawa, Y; Ryu, D; Sato, H; Tomisugi, Y; Tsutsumi, H; Uno, T; Wilkinson, AJ | 1 |
| Chong, KT; Miyazaki, G; Morimoto, H; Park, SY; Shih, DT; Tame, JR; Unzai, S; Yokoyama, T | 1 |
| Blouin, GC; Hargrove, MS; Kundu, S; Olson, JS; Premer, SA; Sarath, G | 1 |
| Berezhna, S; Cao, W; Champion, PM; Demidov, AA; Georgiev, GY; Sage, JT; Sjodin, T; Wang, W; Ye, X | 1 |
| Dewilde, S; Fago, A; Gilany, K; Hundahl, C; Moens, L; Weber, RE | 1 |
| Barrick, D; Berezhna, S; Cao, W; Champion, PM; Christian, JF; Demidov, AA; Sage, JT; Sjodin, T; Wang, W; Ye, X | 1 |
| Hashimoto, Y; Higashibata, H; Ishida, K; Kitagawa, T; Kobayashi, M; Konishi, K; Ohta, T; Oinuma, K | 1 |
| Kitagawa, T; Mogi, T; Nakamura, H; Uchida, T | 1 |
| Amoroso, JH; Baldwin, MJ; Dawson, JH; Gibney, BR; Kinloch, R; Zhuang, J | 1 |
| Kitagawa, T; Sagami, I; Sato, A; Sato, E; Shimizu, T; Uchida, T | 1 |
| Blomberg, LM; Blomberg, MR; Siegbahn, PE | 1 |
| Amadei, A; Anselmi, M; Bossa, C; Brunori, M; Daidone, I; Di Nola, A; Vallone, B | 1 |
| Blouin, G; Dantsker, D; Friedman, JM; Olson, JS; Roche, C; Samuni, U | 1 |
| Kawada, N; Kitagawa, T; Makino, M; Mizutani, Y; Ohta, T; Sawai, H; Shiro, Y; Sugimoto, H; Uno, T; Yoshizato, K | 1 |
| Casella, L; Coletta, M; Dallacosta, C; De Sanctis, G; Fasciglione, GF; Marini, S; Monzani, E; Santucci, R; Sinibaldi, F | 1 |
| Bhaskaran, S; Esquerra, RM; Goldbeck, RA; Kliger, DS; Mendoza, JL; Olson, JS; Ortega, C; Soman, J | 1 |
| Brittain, T; Dewilde, S; Fago, A; Mathews, AJ; Moens, L | 1 |
| Burstyn, JN; Clark, RW; Pinkert, JC | 1 |
| Car, R; De Angelis, F; Jarzecki, AA; Spiro, TG | 1 |
| Aono, S; Nakajima, H; Rubtsov, IV; Yoshihara, K; Zhang, T | 1 |
| Hashimoto, S; Takeuchi, H | 1 |
| Jaffer, N; Jia, Z; Suits, MD | 1 |
| Burstyn, JN; Clark, RW; Lee, AJ; Roberts, GP; Youn, H | 1 |
| Rutkowska-Zbik, D; Stochel, G; Witko, M | 1 |
| Halder, P; Hargrove, MS; Hoy, JA; Smagghe, BJ | 1 |
| Abbruzzetti, S; Bruno, S; Cacciatori, E; Dominici, P; Faggiano, S; Feis, A; Grandi, E; Mackowiak, S; Mozzarelli, A; Smulevich, G; Spyrakis, F; Viappiani, C | 1 |
| Casella, L; Gullotti, M; Monzani, E; Santagostini, L | 1 |
| Goj, A; Loring, RF | 1 |
| Nienhaus, GU; Nienhaus, K; Palladino, P | 1 |
| Arcovito, A; Brunori, M; D'Angelo, P; Della Longa, S; Mancini, G; Moschetti, T; Vallone, B | 1 |
| Burstyn, JN; Kerby, RL; Marvin, KA; Roberts, GP; Youn, H | 1 |
| Althaus, M; Buchäckert, Y; Clauss, WG; Fronius, M; Morty, RE; Motterlini, R; Seeger, W; Vadász, I | 1 |
| Anderson, JL; Dutton, PL; Koder, RL; Moser, CC; Reddy, KS; Solomon, LA | 1 |
| Abbruzzetti, S; Astegno, A; Bidon-Chanal, A; Brogioni, S; Bruno, S; Carrillo, O; Cozzini, P; Dominici, P; Faggiano, S; Feis, A; Grandi, E; Luque, FJ; Mozzarelli, A; Schmidtke, P; Smulevich, G; Spyrakis, F; Viappiani, C | 1 |
| Birukou, I; Olson, JS; Schweers, RL | 1 |
| Anfinrud, P; Cho, HS; Dashdorj, N; Graber, T; Henning, R; Schotte, F | 1 |
| Furutani, Y; Hoshino, T; Ikezaki, A; Imai, K; Kandori, H; Komatsu, T; Nakamura, M; Neya, S; Ode, H; Suzuki, M | 1 |
| Axup, JY; Chung, JK; Fayer, MD; Thielges, MC | 1 |
| Dewilde, S; Geuens, E; Hoogewijs, D; Kiger, L; Lechauve, C; Marden, MC; Moens, L; Tilleman, L | 1 |
| Lutz, S; Meuwly, M | 1 |
| Aono, S; Ishikawa, H; Mizutani, Y; Yoshida, Y | 1 |
| Lecomte, JT; Majumdar, A; Pond, MP | 1 |
| Andersen, EM; Khajo, A; Koder, RL; Magliozzo, RS; Zhang, L | 1 |
| Neya, S | 1 |
| Huang, MJ; Liao, MS; Watts, JD | 1 |
| Alvarez, B; Ballou, DP; Banerjee, R; Carballal, S; Cuevasanta, E; Gherasim, C; Kabil, O; Marmisolle, I | 1 |
| Benabbas, A; Champion, PM; Dawson, JH; Denisov, I; Du, J; Sligar, SG; Sun, Y; Ye, X; Zeng, W | 1 |
| Ishikawa, H; Mizuno, M; Mizutani, Y; Shibayama, N; Yamada, K | 1 |
| Hirota, S; Imai, K; Ishigami, I; Matsuo, T; Nagao, S; Neya, S; Nishimura, R; Ogura, T; Shibata, T; Shoji, O; Suzuki, A; Tai, H; Watanabe, Y; Yamamoto, Y | 1 |
| de Serrano, V; Franzen, S; Zhao, J | 1 |
| Albuquerque, IS; Bernardes, GJ; Carvalho, SM; Chaves-Ferreira, M; Coelho, AC; Matak-Vinkovic, D; Romão, CC; Saraiva, LM | 1 |
| Beckerson, P; Reeder, BJ; Wilson, MT | 1 |
| Bandyopadhyay, P; Kumar, A; Kundu, S; Sharma, S | 1 |
| King, JT; Kubarych, KJ; Pecoraro, VL; Ross, MR; White, AM; Yu, F | 1 |
| Barr, I; Burstyn, JN; Guo, F; Hines, JP; Jacob, JP; Lukat-Rodgers, GS; Rodgers, KR; Smith, AT | 1 |
| Bernad, S; Butcher, D; Derrien, V; Miksovska, J; Sebban, P | 1 |
| Baratto, MC; Fittipaldi, M; Howes, BD; Milazzo, L; Piro, MC; Pogni, R; Santucci, R; Sinibaldi, F; Smulevich, G; Tognaccini, L | 1 |
| Brewitz, HH; Gessner, G; Heimer, P; Heinemann, SH; Hirth, G; Hoshi, T; Imhof, D; Mede, R; Sahoo, N; Schönherr, R; Swain, SM; Westerhausen, M | 1 |
| Ichiyanagi, K; Ohki, M; Park, SY; Sato-Tomita, A; Shibayama, N | 1 |
| Cavazza, C; Contaldo, U; Curtil, M; Le Goff, A; Pérard, J | 1 |
2 review(s) available for histidine and carbon monoxide
| Article | Year |
|---|---|
Hemocyanin--a current perspective.
Topics: Aging; Amino Acids; Animals; Binding Sites; Carbohydrates; Carbon Monoxide; Cations, Divalent; Chemical Phenomena; Chemistry, Physical; Circular Dichroism; Copper; Hemocyanins; Hemolymph; Histidine; Immunoelectrophoresis, Two-Dimensional; Macromolecular Substances; Mathematics; Microscopy, Electron; Molecular Weight; Oxygen; Species Specificity | 1983 |
Dynamic motion and rearranged molecular shape of heme in myoglobin: structural and functional consequences.
Topics: Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Iron; Molecular Structure; Motion; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Oxygen; Rotation | 2013 |
171 other study(ies) available for histidine and carbon monoxide
| Article | Year |
|---|---|
Hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.
Topics: Amino Acid Sequence; Arginine; Carbon Monoxide; Diphosphoglyceric Acids; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Italy; Kinetics; Oxidation-Reduction; Oxygen; Photochemistry | 1975 |
Spectroscopic studies of the nature of ligand bonding in carbonmonoxyhemoglobins: evidence of a specific function for histidine-E7 from infrared and nuclear magnetic resonance intensities.
Topics: Animals; Carbon Monoxide; Carboxyhemoglobin; Hemoglobins; Histidine; Horses; Humans; Ligands; Macromolecular Substances; Magnetic Resonance Spectroscopy; Models, Chemical; Protein Binding; Rabbits; Species Specificity; Spectrophotometry, Infrared | 1978 |
Allosteric interactions in non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and hemoglobin Abruzzo (beta143 (H21) His replaced by Arg).
Topics: Allosteric Regulation; Amino Acid Sequence; Animals; Arginine; Carbon Monoxide; Diphosphoglyceric Acids; Female; Fetal Hemoglobin; Hemoglobins; Hemoglobins, Abnormal; Histidine; Italy; Kinetics; Macromolecular Substances; Oxygen; Phytic Acid; Pregnancy; Protein Binding; Protein Conformation; Time Factors | 1975 |
Hemoglobin Rouen (alpha-140 (HC2) Tyr-->His): alteration of the alpha-chain C-terminal region and moderate increase in oxygen affinity.
Topics: Aged; Aged, 80 and over; Allosteric Regulation; Amino Acids; Carbon Monoxide; Chromatography, High Pressure Liquid; Hemoglobins, Abnormal; Histidine; Humans; Kinetics; Male; Mutation; Oxygen; Polycythemia Vera; Serine Endopeptidases; Tyrosine | 1992 |
Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase.
Topics: Alkenes; Base Sequence; Carbon Monoxide; Cytochrome-c Peroxidase; DNA Mutational Analysis; Ferric Compounds; Ferrous Compounds; Glycine; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Leucine; Ligands; Molecular Sequence Data; Oligonucleotides; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry, Infrared; Spectrum Analysis, Raman; Structure-Activity Relationship; Water | 1991 |
Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66----Thr) and its isolated beta chains.
Topics: Carbon Monoxide; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Molecular; Oxygen; X-Ray Diffraction | 1991 |
Investigations of optical line shapes and kinetic hole burning in myoglobin.
Topics: Carbon Monoxide; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Macromolecular Substances; Mathematics; Myoglobin; Oxygen; Protein Conformation; Spectrophotometry; Spectrum Analysis, Raman; Temperature | 1991 |
Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques.
Topics: Animals; Carbon Monoxide; Histidine; Kinetics; Lasers; Molecular Structure; Mutagenesis, Site-Directed; Myoglobin; Nitric Oxide; Nitriles; Oxygen; Photolysis; Valine; Whales | 1990 |
Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin.
Topics: Allosteric Regulation; Animals; Binding Sites; Carbon Monoxide; Histidine; Hydrogen-Ion Concentration; Kinetics; Myoglobin; Protons; Spectrum Analysis, Raman; Whales | 1989 |
Effect of the distal histidine modification (Cyanation) of myoglobin on the ligand binding kinetics and the heme environmental structures.
Topics: Animals; Carbon Monoxide; Cyanogen Bromide; Heme; Histidine; Ligands; Male; Myoglobin; Spermatozoa; Thermodynamics; Whales | 1989 |
Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine.
Topics: Amino Acid Sequence; Animals; Carbon Monoxide; Escherichia coli; Histidine; Hydrogen Bonding; Kinetics; Mutation; Myoglobin; Oxidation-Reduction; Oxygen; Structure-Activity Relationship; Thermodynamics; Whales | 1989 |
Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts.
Topics: Arginine; Binding Sites; Carbon Monoxide; Cytochrome-c Peroxidase; DNA Mutational Analysis; Heme; Histidine; Hydrogen Bonding; Peroxidases; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry, Infrared; Spectrum Analysis, Raman | 1988 |
Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes.
Topics: Carbon Monoxide; Chloride Peroxidase; Cysteine; Cytochrome-c Peroxidase; Heme; Hemeproteins; Histidine; Horseradish Peroxidase; Imidazoles; Isoenzymes; Lactoperoxidase; Magnetic Resonance Spectroscopy; Myoglobin; Peroxidases | 1985 |
The role of the distal histidine in myoglobin and haemoglobin.
Topics: Animals; Carbon Monoxide; Escherichia coli; Globins; Glycine; Hemoglobins; Histidine; Humans; Hydrogen Bonding; Mutation; Myoglobin; Nitriles; Oxygen; Recombinant Proteins; Structure-Activity Relationship; Whales | 1988 |
Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.
Topics: Animals; Carbon Monoxide; Glycine; Histidine; Kinetics; Ligands; Mutation; Myoglobin; Protein Binding; Thermodynamics; Whales | 1988 |
1H resonances of proximal histidine in CO complexes of hemoglobins provide a sensitive probe of coordination geometry.
Topics: Carbon Monoxide; Hemoglobins; Histidine; Leghemoglobin; Magnetic Resonance Spectroscopy; Myoglobin | 1987 |
Kinetics of carbon monoxide binding to monomeric hemoproteins. Role of the proximal histidine.
Topics: Animals; Carbon Monoxide; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Kinetics; Spectrophotometry; Time Factors | 1985 |
Resonance Raman studies of CO and O2 binding to elephant myoglobin (distal His(E7)----Gln).
Topics: Animals; Carbon Monoxide; Elephants; Glutamine; Histidine; Myoglobin; Oxygen; Spectrum Analysis, Raman; Whales | 1985 |
Carbon monoxide bonding in hemeproteins.
Topics: Binding Sites; Carbon Monoxide; Cytochromes; Electron Transport Complex IV; Heme; Hemoglobins; Histidine; Infrared Rays; Iron; Ketones; Myoglobin; Oxygen; Protein Binding; Proteins; Spectrum Analysis | 1970 |
The physical chemistry of hemes and hemopeptides. I. Physiochemical properties and reduction of chlorodeuterohemin in organic solvent.
Topics: Carbon Monoxide; Chlorine; Deuterium; Electron Spin Resonance Spectroscopy; Esters; Heme; Histidine; Imidazoles; Ligands; Magnetic Resonance Spectroscopy; Mathematics; Methanol; Organometallic Compounds; Oxidation-Reduction; Pyridines; Solvents; Spectrophotometry; Spectrophotometry, Infrared; Sulfites | 1973 |
[The reduction of the B 12 -vitamins by carbon monoxide].
Topics: Benzimidazoles; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Histidine; Hydrogen-Ion Concentration; Kinetics; Lactams; Methanol; Methylation; Oxidation-Reduction; Spectrophotometry; Vitamin B 12 | 1972 |
Molecular conformation and cooperativity in hemoglobin.
Topics: Binding Sites; Carbon Monoxide; Cyanides; Cysteine; Diphosphoglyceric Acids; Fluoroacetates; Fourier Analysis; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Iron Isotopes; Ligands; Magnetic Resonance Spectroscopy; Models, Structural; Oxygen; Oxyhemoglobins; Phosphorus Isotopes; Protein Binding; Protein Conformation; Spectrophotometry; Tyrosine | 1973 |
The ligand-binding properties of hemoglobin Hiroshima ( 2 2 146asp ).
Topics: Amino Acid Sequence; Amino Acids; Aspartic Acid; Butyrates; Carbon Monoxide; Crystallography; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Japan; Kinetics; Ligands; Nitriles; Oxygen; Peptides; Photolysis; Protein Binding; Protein Conformation; Protons; Spectrophotometry; Sulfites | 1972 |
Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin.
Topics: Adult; Binding Sites; Carbon Monoxide; Deuterium; Diphosphoglyceric Acids; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Magnetic Resonance Spectroscopy; Oxygen; Phosphates; Potassium Chloride; Protein Binding; Protein Conformation; Sulfates; Tromethamine; Valine | 1973 |
Ligand binding kinetics of des arginine haemoglobin.
Topics: Allosteric Regulation; Amino Acid Sequence; Arginine; Binding Sites; Carbon Monoxide; Carboxyhemoglobin; Hemoglobins; Histidine; Humans; Kinetics; Ligands; Magnesium; Mathematics; Nitriles; Oxygen; Oxyhemoglobins; Protein Binding; Protein Conformation; Spectrophotometry; Sulfites; Time Factors | 1973 |
The ligand-binding properties of desHis (146beta) hemoglobin.
Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Carbon Monoxide; Carboxyhemoglobin; Carboxypeptidases; Cyanides; Hemoglobins; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Japan; Kinetics; Ligands; Maryland; Mathematics; Oxyhemoglobins; Protein Binding; Protein Conformation; Time Factors | 1973 |
Structure of deoxyhaemoglobin Yakima: a high-affinity mutant form exhibiting oxy-like 1 2 subunit interactions.
Topics: Aspartic Acid; Carbon Monoxide; Crystallization; Glutamates; Hemoglobins, Abnormal; Histidine; Microscopy, Electron; Models, Structural; Oxygen; Peptides; Protein Conformation; Washington; X-Ray Diffraction | 1973 |
Effect of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus.
Topics: Amino Acid Sequence; Amino Acids; Animals; Buffers; Carbon Monoxide; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Kinetics; Leucine; Macromolecular Substances; Organophosphorus Compounds; Oxygen; Primates; Protein Binding; Species Specificity; Spectrophotometry; Spectrophotometry, Ultraviolet | 1974 |
The functional properties of hemoglobin Bethesda ( 2 2 145His ).
Topics: Amino Acids; Binding Sites; Buffers; Carbon Monoxide; Chemical Phenomena; Chemistry; Heme; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Kinetics; Macromolecular Substances; Mutation; Nitriles; Osmolar Concentration; Oxygen; Peptides; Protein Binding; Protein Conformation; Spectrophotometry; Tyrosine; Ultracentrifugation | 1972 |
Interaction of myoglobin and cytochrome C.
Topics: Alkylation; Amobarbital; Animals; Antimycin A; Carbon Monoxide; Cetacea; Chemical Phenomena; Chemistry; Cytochromes; Electron Transport; Histidine; Hydrogen-Ion Concentration; Kinetics; Myoglobin; Oxidation-Reduction; Oxygen; Rotenone; Spectrophotometry; Thermodynamics; Ultraviolet Rays | 1972 |
Reactivity of the 93 sulphydryls of human haemoglobin A: influence of the C-terminal residues.
Topics: Carbon Monoxide; Circular Dichroism; Hemoglobins, Abnormal; Histidine; Humans; Kinetics; Mercuribenzoates; Oxygen; Peptide Chain Termination, Translational; Protein Binding; Protein Conformation; Sulfhydryl Compounds; Tyrosine | 1972 |
Purification and properties of cytochrome c 3 of Desulfovibrio vulgaris, Miyazaki.
Topics: Amino Acids; Carbon Monoxide; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Thin Layer; Cytochromes; Dansyl Compounds; Desulfovibrio; Electron Transport; Heme; Histidine; Hydrogen; Iron; Kinetics; Mathematics; Molecular Weight; Oxidation-Reduction; Oxidoreductases; Potentiometry; Species Specificity; Spectrophotometry; Spectrum Analysis; Sulfites; Ultraviolet Rays | 1971 |
Effect of 2,3-diphosphoglycerate on the Bohr effect of human adult hemoglobin.
Topics: Adult; Carbon Monoxide; Chromatography, Ion Exchange; Glycerophosphates; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Imidazoles; Oxygen; Phosphates; Protein Binding | 1971 |
Alterations in the heme-carbon monoxide bond strength.
Topics: Argon; Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry; Crystallins; Cyclopropanes; Heme; Histidine; Krypton; Lasers; Methods; Myoglobin; Nitrogen; Photolysis; Xenon | 1970 |
Functional properties of hemoglobin Zürich.
Topics: Carbon Monoxide; Chemical Phenomena; Chemistry; Chromatography; Chromatography, Ion Exchange; Cyanides; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Light; Oxygen; Switzerland | 1969 |
Infrared studies of azido, cyano, and other derivatives of metmyoglobin, methemoglobin, and hemins.
Topics: Azides; Carbon Monoxide; Cyanates; Cyanides; Deuterium; Heme; Hemoglobins; Histidine; Hydrogen; Hydrogen-Ion Concentration; Infrared Rays; Myoglobin; Potassium; Sodium; Spectrophotometry; Thiocyanates | 1970 |
Ultraviolet difference spectra in human hemoglobin. I. Difference spectra in hemoglobin A and their relation to the function of hemoglobin.
Topics: Amino Acid Sequence; Animals; Blood; Carbon Monoxide; Chemical Phenomena; Chemistry; Cyanides; Ferricyanides; Fetal Hemoglobin; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Molecular Weight; Oxygen; Peptides; Potassium Chloride; Species Specificity; Spectrophotometry; Swine; Temperature; Tryptophan; Tyrosine; Ultraviolet Rays; Umbilical Cord | 1970 |
The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins.
Topics: Anemia, Hemolytic, Congenital; Binding Sites; Blood Protein Electrophoresis; Carbon Monoxide; Cyanides; Glutathione; Heinz Bodies; Heme; Hemoglobins, Abnormal; Histidine; Hot Temperature; Humans; Methods; Peptides; Protein Binding; Sulfhydryl Compounds | 1970 |
Kinetics of the reaction of hybrid-heme hemoglobins with carbon monoxide.
Topics: Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry; Deuterium; Heme; Hemoglobins; Histidine; Iron; Methemoglobin | 1970 |
The proton-binding behavior of human hemoglobin and its subunits in their native state.
Topics: Acids; Amines; Benzoates; Binding Sites; Carbon Monoxide; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Iron; Lysine; Mercury; Peptides; Protons; Spectrophotometry; Sulfhydryl Compounds; Tyrosine; Water | 1968 |
Urinary excretion of frameshift mutagens in rats caused by passive smoking.
Topics: Air; Animals; Atmosphere Exposure Chambers; Breath Tests; Carbon Monoxide; Diuresis; Histidine; Male; Mutagenicity Tests; Mutagens; Rats; Rats, Inbred Strains; Salmonella typhimurium; Tobacco Smoke Pollution | 1984 |
Nanosecond flash photolysis study of carbon monoxide binding to the beta chain of hemoglobin Zürich [beta 63(E7)His leads to Arg].
Topics: Arginine; Carbon Monoxide; Hemoglobins, Abnormal; Histidine; Humans; Macromolecular Substances; Photolysis; Structure-Activity Relationship; Thermodynamics | 1983 |
The contribution of histidine (HC3) (146 beta) to the R state Bohr effect of human hemoglobin.
Topics: Carbon Dioxide; Carbon Monoxide; Chemical Phenomena; Chemistry, Physical; Hemoglobin A; Histidine; Humans; Hydrogen-Ion Concentration; Oxyhemoglobins | 1982 |
Functional studies on hemoglobin opossum. Conclusions drawn regarding the role of the distal histidine.
Topics: Animals; Carbon Monoxide; Hemoglobin A; Hemoglobins; Hemoglobins, Abnormal; Histidine; Humans; Kinetics; Opossums; Oxygen | 1982 |
Changes in pKa values of individual histidine residues of human hemoglobin upon reaction with carbon monoxide.
Topics: Amino Acid Sequence; Binding Sites; Carbon Monoxide; Carboxyhemoglobin; Chymotrypsin; Hemoglobin A; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Peptide Fragments; Protein Binding; Trypsin | 1980 |
Isomeric incorporation of the haem into monomeric haemoglobins of Chironomus thummi thummi 3. Comparative study of components, I, III and IV.
Topics: Allosteric Regulation; Animals; Carbon Monoxide; Chironomidae; Diptera; Erythrocruorins; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Isomerism; Macromolecular Substances; Magnetic Resonance Spectroscopy; Oxygen | 1980 |
Isomeric incorporation of the haem into monomeric haemoglobins of Chironomus thummi thummi. 1. Isolation of chemically homogeneous haemoglobins. Evidence for the isomerism of the haem in the component III.
Topics: Animals; Carbon Monoxide; Chironomidae; Diptera; Erythrocruorins; Heme; Hemoglobins; Histidine; Isomerism; Larva; Macromolecular Substances; Magnetic Resonance Spectroscopy; Protein Conformation | 1980 |
Isomeric incorporation of the Haem into monomeric haemoglobins of Chironomus thummi thummi. 2. The Bohr effect of the component III explained on a molecular basis and functional differences between the two isomeric structures.
Topics: Allosteric Regulation; Animals; Carbon Monoxide; Chironomidae; Diptera; Erythrocruorins; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Isomerism; Macromolecular Substances; Magnetic Resonance Spectroscopy; Protein Conformation; Thermodynamics | 1980 |
Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin.
Topics: Animals; Carbon Monoxide; Computer Simulation; Crystallography, X-Ray; Flow Injection Analysis; Histidine; Hydrogen Bonding; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Nitric Oxide; Oxidation-Reduction; Oxygen; Phenylalanine; Photolysis; Structure-Activity Relationship; Whales | 1995 |
Resonance Raman spectroscopy reveals novel ligation properties of the porcine myoglobin double mutant H64V/V68H.
Topics: Animals; Binding Sites; Carbon Monoxide; Histidine; Iron; Mutagenesis, Site-Directed; Myoglobin; Protein Engineering; Spectrophotometry; Spectrum Analysis, Raman; Swine | 1995 |
Laser photolysis behavior of ferrous horseradish peroxidase with carbon monoxide and cyanide: effects of mutations in the distal heme pocket.
Topics: Arginine; Base Sequence; Carbon Monoxide; Cyanides; Ferrous Compounds; Heme; Histidine; Horseradish Peroxidase; Kinetics; Lasers; Molecular Sequence Data; Mutagenesis, Site-Directed; Photolysis; Recombinant Proteins; Spectrum Analysis | 1995 |
Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant.
Topics: Animals; Carbon Monoxide; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Imidazoles; Ligands; Models, Molecular; Mutation; Myoglobin; Protein Engineering; Spectrophotometry; Spectrum Analysis; Swine; Valine; X-Rays | 1995 |
Truncated human P450 2D6: expression in Escherichia coli, Ni(2+)-chelate affinity purification, and characterization of solubility and aggregation.
Topics: Amino Acid Sequence; Base Sequence; Carbon Monoxide; Chromatography, Affinity; Cloning, Molecular; Codon; Cytochrome P-450 CYP2D6; Cytochrome P-450 Enzyme System; DNA Primers; Escherichia coli; Histidine; Humans; Iron Chelating Agents; Kinetics; Liver; Macromolecular Substances; Microsomes, Liver; Mixed Function Oxygenases; Molecular Sequence Data; Nickel; Plasmids; Recombinant Proteins; Restriction Mapping; Sequence Tagged Sites; Solubility; Spectrophotometry | 1995 |
The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers.
Topics: Animals; Biophysical Phenomena; Biophysics; Carbon Monoxide; Crystallography, X-Ray; Electrochemistry; Heme; Histidine; Ligands; Models, Molecular; Molecular Structure; Myoglobin; Protein Structure, Tertiary; Spectrophotometry, Infrared; Stereoisomerism; Thermodynamics | 1994 |
Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enz
Topics: Animals; Carbon Monoxide; Cattle; Circular Dichroism; Enzyme Activation; Ferrous Compounds; Glycerol; Guanylate Cyclase; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Nitric Oxide | 1995 |
FT-IR difference spectroscopy of hemoglobins A and Kempsey: evidence that a key quaternary interaction induces protonation of Asp beta 99.
Topics: Adult; Carbon Monoxide; Deuterium; Hemoglobin A; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Protons; Spectroscopy, Fourier Transform Infrared | 1995 |
Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis.
Topics: Azotobacter vinelandii; Base Sequence; Binding Sites; Carbon Monoxide; Catalysis; DNA, Bacterial; Electron Spin Resonance Spectroscopy; Electron Transport; Histidine; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Structure; Molybdoferredoxin; Mutagenesis, Site-Directed; Nitrogen; Nitrogenase; Oxidation-Reduction; Point Mutation; Protons | 1995 |
Identification of histidine 25 as the heme ligand in human liver heme oxygenase.
Topics: Carbon Monoxide; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Ligands; Liver; Oxidation-Reduction; Point Mutation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman | 1994 |
Spectroscopic study of Ser92 mutants of human myoglobin: hydrogen bonding effect of Ser92 to proximal His93 on structure and property of myoglobin.
Topics: Carbon Monoxide; Cyanides; Escherichia coli; Ferric Compounds; Ferrous Compounds; Histidine; Humans; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Mutagenesis; Myoglobin; Oxygen; Polymerase Chain Reaction; Recombinant Fusion Proteins; Serine; Spectrophotometry; Spectrum Analysis, Raman; Structure-Activity Relationship | 1994 |
Cytochrome d axial ligand of the bd-type terminal quinol oxidase from Escherichia coli.
Topics: Binding Sites; Carbon Monoxide; Cytochrome b Group; Cytochrome d Group; Cytochromes; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Histidine; Hydrogen Bonding; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Spectrophotometry, Infrared; Spectrum Analysis, Raman | 1993 |
Structural determinants of the stretching frequency of CO bound to myoglobin.
Topics: Animals; Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry, Physical; Crystallography, X-Ray; Electrochemistry; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Structure; Mutagenesis, Site-Directed; Myoglobin; Phenylalanine; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Swine; Whales | 1994 |
Effects of intra- and intersubunit hydrogen bonds on the R-T transition in human hemoglobin as studied with alpha 42(C7) and beta 145(HC2) mutations.
Topics: Amino Acid Sequence; Aspartic Acid; Carbon Monoxide; Escherichia coli; Hemoglobin A; Histidine; Humans; Hydrogen Bonding; Kinetics; Macromolecular Substances; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Thermodynamics; Tyrosine | 1993 |
Heme-heme interactions in a homodimeric cooperative hemoglobin. Evidence from transient Raman scattering.
Topics: Animals; Bivalvia; Carbon Monoxide; Heme; Hemoglobins; Histidine; Iron; Protein Conformation; Spectrum Analysis, Raman | 1993 |
Time-resolved resonance Raman study on the binding of carbon monoxide to recombinant human myoglobin and its distal histidine mutants.
Topics: Carbon Monoxide; Chemical Phenomena; Chemistry, Physical; Histidine; Humans; Kinetics; Lasers; Mutagenesis, Site-Directed; Myoglobin; Photochemistry; Recombinant Proteins; Spectrum Analysis, Raman | 1993 |
Site-directed mutagenesis in hemoglobin. Effect of some mutations at protein interfaces.
Topics: Allosteric Regulation; Arginine; Carbon Monoxide; Hemoglobin A; Histidine; Humans; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Oxygen; Protein Conformation; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Threonine; Tryptophan; Valine | 1993 |
Crystal structures of CO-, deoxy- and met-myoglobins at various pH values.
Topics: Animals; Anisotropy; Carbon Monoxide; Computer Graphics; Crystallization; Crystallography, X-Ray; Heme; Histidine; Hydrogen-Ion Concentration; Metmyoglobin; Models, Molecular; Myoglobin; Protein Conformation; Protein Structure, Tertiary; Whales | 1996 |
Global mapping of structural solutions provided by the extended X-ray absorption fine structure ab initio code FEFF 6.01: structure of the cryogenic photoproduct of the myoglobin-carbon monoxide complex.
Topics: Animals; Carbon Monoxide; Computer Simulation; Crystallography, X-Ray; Heme; Histidine; Horses; Iron; Muscle, Skeletal; Myoglobin; Photolysis; Software; Spectrophotometry; Spectrum Analysis, Raman; Temperature | 1996 |
Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine alpha-amidating enzyme.
Topics: Animals; Binding Sites; Carbon Monoxide; CHO Cells; Cloning, Molecular; Copper; Cricetinae; Electron Spin Resonance Spectroscopy; Histidine; Mixed Function Oxygenases; Multienzyme Complexes; Oligopeptides; Oxidation-Reduction; Protein Conformation; Rats; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; X-Rays | 1996 |
Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography.
Topics: Carbon Monoxide; Computer Simulation; Crystallography, X-Ray; Fourier Analysis; Globins; Heme; Histidine; Iron; Ligands; Myoglobin; Photolysis; Temperature; Time Factors | 1996 |
Theoretical study of the electrostatic and steric effects on the spectroscopic characteristics of the metal-ligand unit of heme proteins. 2. C-O vibrational frequencies, 17O isotropic chemical shifts, and nuclear quadrupole coupling constants.
Topics: Carbon Monoxide; Heme; Hemeproteins; Hemoglobins; Histidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; Myoglobin; Oxygen; Oxygen Isotopes; Porphyrins; Protein Conformation | 1997 |
Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Carbon Monoxide; Cloning, Molecular; Crystallography, X-Ray; Fabaceae; Glycine max; Hemin; Histidine; Leghemoglobin; Ligands; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nitric Oxide; Oxidation-Reduction; Oxygen; Plant Roots; Plants, Medicinal; Protein Conformation; Recombinant Proteins; Species Specificity; Structure-Activity Relationship | 1997 |
Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy.
Topics: Animals; Carbon Monoxide; Heme; Histidine; Horses; Iron; Ligands; Myoglobin; Pressure; Protein Conformation; Spectrophotometry, Infrared; Spectrum Analysis, Raman; Temperature | 1997 |
Glutamate-286 mutants of cytochrome bo-type ubiquinol oxidase from Escherichia coli: influence of mutations on the binuclear center structure revealed by FT-IR and EPR spectroscopies.
Topics: Binding Sites; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Escherichia coli; Glutamic Acid; Histidine; Mutagenesis, Site-Directed; Oxidation-Reduction; Point Mutation; Proline; Protein Conformation; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared | 1997 |
The apolar distal histidine mutant (His69-->Val) of the homodimeric Scapharca hemoglobin is in an R-like conformation.
Topics: Amino Acid Substitution; Animals; Bivalvia; Carbon Monoxide; Circular Dichroism; Dimerization; Heme; Hemoglobins; Histidine; Ligands; Mutagenesis, Insertional; Protein Binding; Protein Conformation; Spectrophotometry; Spectrum Analysis, Raman; Valine | 1998 |
Influence of proximal side mutations on the molecular and electronic structure of cyanomet myoglobin: an 1H NMR study.
Topics: Animals; Binding Sites; Carbon Monoxide; Energy Transfer; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Male; Metmyoglobin; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protons; Spermatozoa; Whales | 1998 |
Synergistic activation of soluble guanylate cyclase by YC-1 and carbon monoxide: implications for the role of cleavage of the iron-histidine bond during activation by nitric oxide.
Topics: Carbon Monoxide; Enzyme Activation; Guanylate Cyclase; Histidine; Hydrolysis; Indazoles; Iron; Kinetics; Nitric Oxide | 1998 |
The distal cavity structure of carbonyl horseradish peroxidase as probed by the resonance Raman spectra of His 42 Leu and Arg 38 Leu mutants.
Topics: Amino Acid Substitution; Arginine; Carbon Monoxide; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Isoenzymes; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Spectrum Analysis, Raman | 1998 |
Resonance raman characterization of the heme domain of soluble guanylate cyclase.
Topics: Animals; Carbon Monoxide; Ferrous Compounds; Glycine; Guanylate Cyclase; Heme; Histidine; Imidazoles; Lung; Nitric Oxide; Peptide Fragments; Protein Structure, Tertiary; Rats; Solubility; Spectrum Analysis, Raman | 1998 |
X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
Topics: Amino Acid Sequence; Binding Sites; Carbon Monoxide; Catalytic Domain; Clostridium; Crystallography, X-Ray; Cyanides; Cysteine; Histidine; Hydrogen; Hydrogenase; Iron; Ligands; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protons; Sulfur | 1998 |
Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Carbon Monoxide; Cysteine; Escherichia coli; Ferric Compounds; Ferrous Compounds; Heme; Hemeproteins; Histidine; Ligands; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Rhodospirillum rubrum; Trans-Activators | 1999 |
A steric mechanism for inhibition of CO binding to heme proteins.
Topics: Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Hydrogen Bonding; Iron; Ligands; Metmyoglobin; Models, Molecular; Myoglobin; Nitrogen; Protein Conformation; Protein Structure, Secondary; Temperature; Valine | 1999 |
Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor?
Topics: Animals; Bromides; Carbon Monoxide; Cattle; Chlorides; Copper; Cytochrome b Group; Cytochromes; Escherichia coli; Escherichia coli Proteins; Fourier Analysis; Histidine; Imidazoles; Ligands; Oxidation-Reduction; Photolysis; Spectrometry, X-Ray Emission | 1999 |
Internal electron transfer and structural dynamics of cd1 nitrite reductase revealed by laser CO photodissociation.
Topics: Alanine; Binding Sites; Carbon Monoxide; Cytochrome c Group; Cytochromes; Electron Transport; Histidine; Kinetics; Lasers; Mutagenesis, Site-Directed; Nitrite Reductases; Oxidation-Reduction; Photolysis; Pseudomonas aeruginosa; Spectrophotometry; Thermodynamics; Titrimetry | 1999 |
A study of vibrational relaxation of B-state carbon monoxide in the heme pocket of photolyzed carboxymyoglobin.
Topics: Animals; Carbon Monoxide; Computer Simulation; Heme; Histidine; Myoglobin; Static Electricity; Whales | 1999 |
On the significance of hydrogen bonds for the discrimination between CO and O2 by myoglobin.
Topics: Carbon Monoxide; Computer Simulation; Histidine; Hydrogen Bonding; Imidazoles; Iron; Models, Molecular; Myoglobin; Oxygen; Porphyrins; Vibration | 1999 |
Crystal structures of myoglobin-ligand complexes at near-atomic resolution.
Topics: Animals; Anisotropy; Binding Sites; Carbon Monoxide; Crystallization; Crystallography, X-Ray; Electrons; Heme; Histidine; Hydrogen Bonding; Ligands; Metmyoglobin; Models, Molecular; Myoglobin; Oxygen; Protein Conformation; Protons; Water; Whales | 1999 |
Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity.
Topics: Alanine; Animals; Binding Sites; Carbon Isotopes; Carbon Monoxide; Catalytic Domain; CHO Cells; Copper; Cricetinae; Histidine; Mixed Function Oxygenases; Multienzyme Complexes; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; Substrate Specificity; Superoxides; X-Rays | 1999 |
Spectroscopic characterization of the heme-binding sites in Plasmodium falciparum histidine-rich protein 2.
Topics: Animals; Binding Sites; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Plasmodium falciparum; Proteins; Protozoan Proteins; Spectrophotometry; Spectrum Analysis, Raman | 1999 |
Identification of the proximal ligand His-20 in heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Oxidative cleavage of the heme macrocycle does not require the proximal histidine.
Topics: Bacterial Proteins; Biliverdine; Carbon Monoxide; Catalytic Domain; Chromatography, High Pressure Liquid; Corynebacterium diphtheriae; Electrophoresis, Polyacrylamide Gel; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Histidine; Humans; Hydroxylation; Ligands; Membrane Proteins; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Spectrophotometry, Atomic; Spectrum Analysis, Raman; Structure-Activity Relationship | 2000 |
Altering the specificity of CooA, the carbon monoxide-sensing transcriptional activator: characterization of CooA variants that bind cyanide in the Fe(II) form with high affinity.
Topics: Bacterial Proteins; Carbon Monoxide; Cyanides; Escherichia coli; Escherichia coli Proteins; Ferric Compounds; Ferrous Compounds; Fimbriae Proteins; Histidine; Hydrogen-Ion Concentration; Recombinant Proteins; Transcriptional Activation | 2000 |
Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy.
Topics: Bacterial Proteins; Carbon Monoxide; Escherichia coli; Escherichia coli Proteins; Fimbriae Proteins; Heme; Histidine; Imidazoles; Iron; Ligands; Mutagenesis, Site-Directed; Myoglobin; Photolysis; Spectrum Analysis, Raman; Tyrosine | 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 |
Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam.
Topics: Benzene Derivatives; Camphor; Camphor 5-Monooxygenase; Carbon Monoxide; Catalytic Domain; Cysteine; Ferric Compounds; Ferrous Compounds; Histidine; Ligands; Mutation; Protein Folding; Spectrophotometry | 2001 |
Structural and dynamic perturbations induced by heme binding in cytochrome b5.
Topics: Alanine; Amino Acid Substitution; Animals; Apoproteins; Carbon Monoxide; Crystallography, X-Ray; Cytochrome b Group; Cytochromes b; Cytochromes b5; Heme; Histidine; Macromolecular Substances; Methylamines; Nuclear Magnetic Resonance, Biomolecular; Oxidants; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Rats; Thermodynamics | 2001 |
A photolysis-triggered heme ligand switch in H93G myoglobin.
Topics: Animals; Carbon Monoxide; Ferrous Compounds; Glycine; Heme; Histidine; Iron; Lasers; Ligands; Metmyoglobin; Mutagenesis, Insertional; Myoglobin; Photolysis; Protein Binding; Spectrum Analysis, Raman; Thermodynamics; Whales | 2001 |
Influence of the heme pocket conformation on the structure and vibrations of the Fe-CO bond in myoglobin: a QM/MM density functional study.
Topics: Carbon Monoxide; Computer Simulation; Heme; Histidine; Iron; Ligands; Models, Molecular; Myoglobin; Protein Conformation; Thermodynamics; Vibration | 2001 |
19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant.
Topics: Animals; Carbon Monoxide; Cysteine; Dithionite; Fluorine; Glycine; Histidine; Ligands; Metmyoglobin; Mutagenesis, Site-Directed; Myoglobin; Nitric Oxide; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protons; Sulfhydryl Compounds; Trifluoroacetic Acid; Whales | 2001 |
Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family.
Topics: Animals; Carbon Monoxide; Chromatography, High Pressure Liquid; Cloning, Molecular; Globins; Histidine; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Light; Mice; Models, Molecular; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Oxygen; Protein Binding; Recombinant Proteins; Temperature; Time Factors; Ultracentrifugation | 2001 |
A common inhibitory binding site for zinc and odorants at the voltage-gated K(+) channel of rat olfactory receptor neurons.
Topics: 4-Chloromercuribenzenesulfonate; Acetophenones; Animals; Binding Sites; Carbon Monoxide; Cells, Cultured; Cyclohexenes; Cysteine; Diethyl Pyrocarbonate; Dose-Response Relationship, Drug; Histidine; Limonene; Membrane Potentials; Mesylates; Neural Inhibition; Nitric Oxide; Olfactory Receptor Neurons; Patch-Clamp Techniques; Pentanols; Potassium; Potassium Channels; Rats; Receptors, Odorant; Smell; Sulfhydryl Reagents; Terpenes; Zinc | 2001 |
Interaction of acetylene and cyanide with the resting state of nitrogenase alpha-96-substituted MoFe proteins.
Topics: Acetylene; Amino Acid Substitution; Arginine; Azotobacter vinelandii; Binding Sites; Carbon Monoxide; Catalytic Domain; Cyanides; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Glutamine; Histidine; Leucine; Molybdoferredoxin; Nitrogenase; Substrate Specificity; Thermodynamics | 2001 |
Observation of an isotope-sensitive low-frequency Raman band specific to metmyoglobin.
Topics: Animals; Carbon Monoxide; Histidine; Iron; Isotope Labeling; Methemoglobin; Metmyoglobin; Myoglobin; Protein Subunits; Recombinant Proteins; Spectrum Analysis, Raman; Whales | 2002 |
The carbon monoxide derivative of human hemoglobin carrying the double mutation LeuB10-->Tyr and HisE7-->Gln on alpha and beta chains probed by infrared spectroscopy.
Topics: Amino Acid Substitution; Carbon Monoxide; Carboxyhemoglobin; Glutamine; Heme; Hemoglobin A; Histidine; Humans; Hydrogen Bonding; Iron; Kinetics; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Tyrosine | 2002 |
Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli.
Topics: Carbon Monoxide; Carrier Proteins; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Methionine; Mutation; Oxygen; Phosphoric Diester Hydrolases; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Time Factors | 2002 |
Characterization of the relevant excited states in the photodissociation of CO-ligated hemoglobin and myoglobin.
Topics: Carbon Monoxide; Carboxyhemoglobin; Hemoglobins; Histidine; Humans; Imidazoles; Models, Chemical; Models, Molecular; Molecular Mimicry; Myoglobin; Photochemistry; Porphyrins; Thermodynamics | 2002 |
Kinetic barriers to the folding of horse cytochrome C in the reduced state.
Topics: Animals; Binding Sites; Carbon Monoxide; Cytochrome c Group; Enzyme Stability; Ferrous Compounds; Guanidine; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Methionine; Models, Chemical; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2002 |
The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant.
Topics: Alanine; Animals; Binding Sites; Carbon Monoxide; Catalysis; CHO Cells; Copper; Cricetinae; Enzyme Activation; Histidine; Imidazoles; Ligands; Mixed Function Oxygenases; Multienzyme Complexes; Oligopeptides; Oxidation-Reduction; Recombinant Proteins; Spectrometry, X-Ray Emission; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; Substrate Specificity; X-Rays | 2002 |
NO-induced activation mechanism of the heme-regulated eIF2alpha kinase.
Topics: Carbon Monoxide; eIF-2 Kinase; Electron Spin Resonance Spectroscopy; Enzyme Activation; Heme; Histidine; Nitric Oxide; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman | 2002 |
Direct infrared detection of the covalently ring linked His-Tyr structure in the active site of the heme-copper oxidases.
Topics: Binding Sites; Carbon Monoxide; Cytochrome b Group; Cytochromes; Dimerization; Escherichia coli Proteins; Free Radicals; Hemeproteins; Histidine; Models, Chemical; Models, Molecular; Oxidoreductases; Spectrophotometry, Infrared; Tyrosine | 2002 |
Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin.
Topics: Amino Acids; Animals; Binding Sites; Carbon Monoxide; Cyanides; Glycine max; Heme; Histidine; Leghemoglobin; Ligands; Models, Molecular; Mutation; Myoglobin; Oxygen; Protein Conformation; Soybean Proteins; Thermodynamics; Water; Whales | 2003 |
YC-1 facilitates release of the proximal His residue in the NO and CO complexes of soluble guanylate cyclase.
Topics: Animals; Carbon Monoxide; Cattle; Electron Spin Resonance Spectroscopy; Guanylate Cyclase; Histidine; Indazoles; Nitric Oxide | 2003 |
1H NMR structure of the heme pocket of HNO-myoglobin.
Topics: Animals; Binding Sites; Carbon Monoxide; Heme; Histidine; Horses; Models, Molecular; Muscle, Skeletal; Myoglobin; Nitrogen Oxides; Nuclear Magnetic Resonance, Biomolecular; Protons | 2003 |
Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations.
Topics: Arginine; Binding Sites; Carbon Monoxide; Heme; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Models, Molecular; Movement; Solvents; Spectrophotometry, Infrared; Temperature | 2003 |
Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Carbon Monoxide; Cloning, Molecular; DNA; Electrophoresis, Polyacrylamide Gel; Globins; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Models, Chemical; Molecular Sequence Data; Mutation; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrophotometry; Spectrum Analysis, Raman; Time Factors | 2004 |
Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect.
Topics: Allosteric Site; Amino Acid Sequence; Animals; Carbon Monoxide; Crystallography, X-Ray; DNA, Complementary; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Ligands; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxygen; Protein Conformation; Sequence Homology, Amino Acid; Tuna | 2004 |
Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin.
Topics: Animals; Carbon Monoxide; Glycine max; Histidine; Hydrogen Bonding; Imidazoles; Leghemoglobin; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Oxygen; Protein Binding; Spectroscopy, Fourier Transform Infrared; Tyrosine; Whales | 2004 |
Proximal and distal influences on ligand binding kinetics in microperoxidase and heme model compounds.
Topics: Animals; Carbon Monoxide; Heart; Heme; Histidine; Horses; Imidazoles; Kinetics; Ligands; Models, Molecular; Myoglobin; Peroxidases; Photolysis; Protein Binding; Protein Conformation; Protoporphyrins; Spectrum Analysis, Raman; Time Factors | 2004 |
Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance.
Topics: Allosteric Site; Animals; Carbon Monoxide; Chromatography, Gel; Chromatography, Ion Exchange; Cytoglobin; Dimerization; Disulfides; Globins; Histidine; Hot Temperature; Humans; Hydrogen-Ion Concentration; Ligands; Lysine; Mass Spectrometry; Mice; Mitochondria; Mutation; Nerve Tissue Proteins; Neuroglobin; Neurons; Oxygen; Protein Binding; Pyridines; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Temperature; Time Factors | 2004 |
Investigations of photolysis and rebinding kinetics in myoglobin using proximal ligand replacements.
Topics: Amino Acid Substitution; Animals; Bromine; Carbon Monoxide; Glycine; Heme; Histidine; Imidazoles; Kinetics; Ligands; Models, Chemical; Myoglobin; Photolysis; Protein Binding; Pyridines; Spectrophotometry; Spectrum Analysis, Raman; Whales | 2004 |
Identification of crucial histidines involved in carbon-nitrogen triple bond synthesis by aldoxime dehydratase.
Topics: Amino Acid Sequence; Bacterial Proteins; Carbon; Carbon Monoxide; Circular Dichroism; Histidine; Hydro-Lyases; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Nitrogen; Oximes; Protein Conformation; Recombinant Proteins; Sequence Alignment; Spectrum Analysis, Raman; Water | 2004 |
Role of Tyr-288 at the dioxygen reduction site of cytochrome bo studied by stable isotope labeling and resonance raman spectroscopy.
Topics: Carbon Monoxide; Catalysis; Copper; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen; Ions; Kinetics; Metals; Models, Chemical; Models, Molecular; Nitrites; Oxygen; Quinone Reductases; Spectrophotometry; Spectrum Analysis, Raman; Temperature; Tyrosine | 2004 |
Design of a five-coordinate heme protein maquette: a spectroscopic model of deoxymyoglobin.
Topics: Carbon Monoxide; Circular Dichroism; Hemeproteins; Histidine; Iron; Methylhistidines; Models, Molecular; Myoglobin; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Thermodynamics | 2004 |
CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2.
Topics: Amino Acid Sequence; Animals; Basic Helix-Loop-Helix Transcription Factors; Carbon Monoxide; Cysteine; Cytochrome c Group; Dimerization; DNA; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Ligands; Liver; Mice; Mice, Inbred C57BL; Models, Chemical; Molecular Sequence Data; Mutation; Nerve Tissue Proteins; Neurons; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Sequence Homology, Amino Acid; Signal Transduction; Spectrum Analysis, Raman; Time Factors; Transcription Factors | 2005 |
A theoretical study on the binding of O(2), NO and CO to heme proteins.
Topics: Benzene; Binding Sites; Carbon Monoxide; Copper; Electron Transport Complex IV; Hemeproteins; Histidine; Models, Chemical; Myoglobin; Nitric Oxide; Oxygen; Porphyrins; Thermodynamics | 2005 |
Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities.
Topics: Animals; Biophysics; Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Iron; Ligands; Light; Models, Molecular; Models, Statistical; Molecular Conformation; Mutation; Myoglobin; Oxygen; Photolysis; Protein Binding; Protein Conformation; Protein Structure, Secondary; Solvents; Whales | 2005 |
The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.
Topics: Animals; Binding Sites; Carbon Monoxide; Glycerol; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Chemical; Models, Molecular; Molecular Conformation; Mutation; Myocardium; Myoglobin; Phase Transition; Protein Binding; Protein Conformation; Recombination, Genetic; Sperm Whale; Stereoisomerism; Temperature; Time Factors; Xenon | 2005 |
Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.
Topics: Carbon Monoxide; Crystallography; Cytoglobin; Globins; Heme; Histidine; Humans; Iron; Ligands; Light; Models, Chemical; Mutation; Nerve Tissue Proteins; Neuroglobin; Nitric Oxide; Photolysis; Protein Binding; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman | 2005 |
pH-dependent redox and CO binding properties of chelated protoheme-L-histidine and protoheme-glycyl-L-histidine complexes.
Topics: Carbon Monoxide; Chelating Agents; Dipeptides; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Thermodynamics | 2006 |
Water and ligand entry in myoglobin: assessing the speed and extent of heme pocket hydration after CO photodissociation.
Topics: Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Electrons; Heme; Histidine; Kinetics; Ligands; Models, Chemical; Models, Molecular; Mutation; Myoglobin; Recombinant Proteins; Spectrophotometry; Sperm Whale; Temperature; Thermodynamics; Time Factors; Water; X-Rays | 2006 |
The reactions of neuroglobin with CO: evidence for two forms of the ferrous protein.
Topics: Animals; Carbon Monoxide; Globins; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Mice; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Protein Conformation | 2006 |
Modeling proline ligation in the heme-dependent CO sensor, CooA, using small-molecule analogs.
Topics: Bacterial Proteins; Carbon Monoxide; Computational Biology; Crystallography, X-Ray; Heme; Hemeproteins; Histidine; Imidazoles; Iron; Ligands; Models, Molecular; Molecular Structure; Proline; Pyrrolidines; Trans-Activators | 2006 |
Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin.
Topics: Animals; Binding Sites; Carbon; Carbon Monoxide; Heme; Histidine; Isoleucine; Models, Molecular; Molecular Conformation; Myoglobin; Oxygen; Photochemistry; Protein Binding; Quantum Theory; Software | 2005 |
Effect of mutation on the dissociation and recombination dynamics of CO in transcriptional regulator CooA: a picosecond infrared transient absorption study.
Topics: Bacterial Proteins; Carbon Monoxide; Glycine; Heme; Hemeproteins; Histidine; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Recombination, Genetic; Regulatory Elements, Transcriptional; Rhodospirillum rubrum; Spectroscopy, Near-Infrared; Trans-Activators | 2006 |
Protonation and hydrogen-bonding state of the distal histidine in the CO complex of horseradish peroxidase as studied by ultraviolet resonance Raman spectroscopy.
Topics: Binding Sites; Carbon Monoxide; Deuterium Oxide; Histidine; Horseradish Peroxidase; Hydrogen Bonding; Imidazoles; Protons; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman | 2006 |
Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193.
Topics: Alanine; Carbon Monoxide; Catalysis; Chromatography, Gas; Crystallography, X-Ray; Escherichia coli O157; Escherichia coli Proteins; Heme; Heme Oxygenase (Decyclizing); Histidine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; X-Ray Diffraction | 2006 |
DNA binding by an imidazole-sensing CooA variant is dependent on the heme redox state.
Topics: Bacterial Proteins; Carbon Monoxide; Circular Dichroism; DNA-Binding Proteins; Gene Expression Regulation, Bacterial; Heme; Hemeproteins; Histidine; Imidazoles; Oxidation-Reduction; Rhodospirillum rubrum; Trans-Activators | 2007 |
Theoretical density functional theory studies on interactions of small biologically active molecules with isolated heme group.
Topics: Carbon Monoxide; Computational Biology; Ferrous Compounds; Heme; Histidine; Ligands; Models, Molecular; Molecular Conformation; Nitric Oxide; Nitrogen Dioxide; Water | 2007 |
Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.
Topics: Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Cyanides; Guanidine; Heme; Hemoglobins; Histidine; Iron; Ligands; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Synechocystis | 2007 |
The reactivity with CO of AHb1 and AHb2 from Arabidopsis thaliana is controlled by the distal HisE7 and internal hydrophobic cavities.
Topics: Arabidopsis; Arabidopsis Proteins; Binding Sites; Carbon Monoxide; Hemoglobins; Histidine; Hydrophobic and Hydrophilic Interactions; Iron; Kinetics; Ligands; Protein Binding; Protein Conformation | 2007 |
Effect of strain in the proximal ligand on the binding of nitric oxide and carbon monoxide to chelated protoheme complexes.
Topics: Carbon Monoxide; Dimethyl Sulfoxide; Dose-Response Relationship, Drug; Heme; Histidine; Imidazoles; Iron; Ligands; Methanol; Models, Chemical; Molecular Structure; Nitric Oxide; Stress, Mechanical; Thermodynamics | 2007 |
Comment on "ultrafast dynamics of myoglobin without the distal histidine: stimulated vibrational echo experiments and molecular dynamics simulations".
Topics: Carbon Monoxide; Computer Simulation; Histidine; Models, Chemical; Myoglobin; Sensitivity and Specificity; Spectrophotometry, Infrared; Thermodynamics; Vibration; Water | 2007 |
Structural dynamics of myoglobin: FTIR-TDS study of NO migration and binding.
Topics: Amino Acid Substitution; Animals; Binding Sites; Carbon Monoxide; Cold Temperature; Darkness; Histidine; Hydrogen-Ion Concentration; Iron; Lasers; Light; Myoglobin; Nitric Oxide; Oxidation-Reduction; Photochemistry; Photolysis; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Sperm Whale; Static Electricity; Thermodynamics; Water | 2008 |
An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin.
Topics: Animals; Carbon Monoxide; Cloning, Molecular; Escherichia coli; Globins; Heme; Histidine; Iron; Mice; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Spectrum Analysis; X-Ray Diffraction; X-Rays | 2008 |
The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch.
Topics: Bacterial Proteins; Burkholderia; Carbon Monoxide; Cysteine; DNA-Binding Proteins; Electron Spin Resonance Spectroscopy; Hemeproteins; Histidine; Iron; Molecular Structure; Nitric Oxide; Oxidation-Reduction; Protein Binding; Spectrum Analysis, Raman; Trans-Activators | 2008 |
Carbon monoxide rapidly impairs alveolar fluid clearance by inhibiting epithelial sodium channels.
Topics: Acute Lung Injury; Amiloride; Animals; Body Fluids; Boranes; Carbon Monoxide; Carbonates; Cell Line; Cyclic GMP; Energy Metabolism; Epithelial Sodium Channel Blockers; Epithelial Sodium Channels; Guanylate Cyclase; Heme Oxygenase-1; Histidine; Humans; In Vitro Techniques; Ion Transport; Organometallic Compounds; Pulmonary Alveoli; Rabbits; Rats; Respiratory Distress Syndrome; Signal Transduction; Sodium-Potassium-Exchanging ATPase | 2009 |
Design and engineering of an O(2) transport protein.
Topics: Biological Transport; Carbon Monoxide; Carrier Proteins; Drug Design; Globins; Glutamic Acid; Heme; Histidine; Humans; Kinetics; Ligands; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Oxygen; Protein Engineering; Protein Structure, Secondary; Rotation; Spectroscopy, Fourier Transform Infrared; Substrate Specificity; Water | 2009 |
Structural plasticity and functional implications of internal cavities in distal mutants of type 1 non-symbiotic hemoglobin AHb1 from Arabidopsis thaliana.
Topics: Absorption; Arabidopsis; Arabidopsis Proteins; Carbon Monoxide; Hemoglobins; Histidine; Kinetics; Lasers; Ligands; Molecular Dynamics Simulation; Mutant Proteins; Mutation; Phenylalanine; Photolysis; Protein Conformation; Protein Stability; Spectrum Analysis, Raman; Time Factors | 2009 |
Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin.
Topics: Carbon Monoxide; Hemoglobins; Histidine; Humans; Hydrogen Bonding; Imidazoles; Kinetics; Ligands; Mutation; Nitric Oxide; Oxygen; Phenylalanine; Protein Binding; Protein Conformation; Thermodynamics | 2010 |
Protein structural dynamics in solution unveiled via 100-ps time-resolved x-ray scattering.
Topics: Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Histidine; Kinetics; Lasers; Models, Molecular; Myoglobin; Photons; Proteins; Scattering, Radiation; Sperm Whale; Temperature; X-Rays | 2010 |
Molecular insight into intrinsic heme distortion in ligand binding in hemoprotein.
Topics: Carbon Monoxide; Heme; Hemeproteins; Histidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Myoglobin; Nitric Oxide; Oxygen; Water | 2010 |
Influence of histidine tag attachment on picosecond protein dynamics.
Topics: Amino Acid Sequence; Animals; Carbon Monoxide; Histidine; Molecular Dynamics Simulation; Molecular Sequence Data; Myoglobin; Protein Binding; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Sperm Whale; Static Electricity; Time Factors | 2011 |
Electron transfer function versus oxygen delivery: a comparative study for several hexacoordinated globins across the animal kingdom.
Topics: Amino Acid Sequence; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Carbon Monoxide; Cytochromes c; Cytoglobin; Electron Transport; Globins; Heme; Histidine; Humans; Iron; Kinetics; Nerve Tissue Proteins; Neuroglobin; Oxygen; Protein Structure, Quaternary; Protein Structure, Tertiary | 2011 |
Structural characterization of spectroscopic substates in carbonmonoxy neuroglobin.
Topics: Animals; Carbon Monoxide; Chemistry, Physical; Globins; Heme; Histidine; Humans; Hydrogen Bonding; Mice; Molecular Dynamics Simulation; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Protein Conformation; Protons; Quantum Theory; Spectrophotometry, Infrared; Stereoisomerism; Thermodynamics | 2011 |
Structural dynamics of proximal heme pocket in HemAT-Bs associated with oxygen dissociation.
Topics: Bacillus subtilis; Bacterial Proteins; Carbon Monoxide; Escherichia coli; Gene Expression; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Iron; Kinetics; Oxygen; Protein Structure, Tertiary; Recombinant Fusion Proteins; Signal Transduction; Spectrum Analysis, Raman | 2012 |
Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin.
Topics: Bacterial Proteins; Carbon Monoxide; Cyanides; Heme; Histidine; Molecular Dynamics Simulation; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Synechococcus; Truncated Hemoglobins | 2012 |
Dynamic factors affecting gaseous ligand binding in an artificial oxygen transport protein.
Topics: Binding Sites; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Globins; Glutamic Acid; Heme; Histidine; Kinetics; Ligands; Mutant Proteins; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Protein Binding; Protein Conformation; Protein Engineering; Protein Folding; Recombinant Proteins; Water | 2013 |
Effects of local protein environment on the binding of diatomic molecules to heme in myoglobins. DFT and dispersion-corrected DFT studies.
Topics: Amino Acid Motifs; Binding Sites; Carbon Monoxide; Heme; Histidine; Humans; Hydrogen Bonding; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Myoglobin; Oxygen; Protein Binding; Quantum Theory; Thermodynamics | 2013 |
Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.
Topics: Carbon Monoxide; Cystathionine beta-Synthase; Cysteine; Heme; Histidine; Humans; Kinetics; Ligands; Oxygen; Protein Binding; Protein Carbonylation; Signal Transduction; Spectrum Analysis, Raman; Sulfur Dioxide; Superoxides | 2013 |
Investigations of heme ligation and ligand switching in cytochromes p450 and p420.
Topics: Camphor 5-Monooxygenase; Carbon Monoxide; Cytochrome P-450 Enzyme System; Heme; Histidine; Ligands; Models, Molecular; Myoglobin; Protein Conformation; Spectrum Analysis, Raman | 2013 |
Intersubunit communication via changes in hemoglobin quaternary structures revealed by time-resolved resonance Raman spectroscopy: direct observation of the Perutz mechanism.
Topics: Carbon Monoxide; Heme; Hemoglobins; Histidine; Humans; Iron; Models, Molecular; Nickel; Protein Structure, Quaternary; Protein Subunits; Spectrum Analysis, Raman; Time Factors | 2013 |
Electronic control of discrimination between O2 and CO in myoglobin lacking the distal histidine residue.
Topics: Animals; Carbon Monoxide; Electrons; Heme; Histidine; Mutant Proteins; Mutation; Myoglobin; Oxygen; Substrate Specificity; Vibration | 2014 |
A model for the flexibility of the distal histidine in dehaloperoxidase-hemoglobin A based on X-ray crystal structures of the carbon monoxide adduct.
Topics: Amino Acid Sequence; Carbon Monoxide; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Hemoglobin A; Hemoglobins; Histidine; Molecular Sequence Data; Peroxidases; Protein Conformation | 2014 |
Spontaneous CO release from Ru(II)(CO)2-protein complexes in aqueous solution, cells, and mice.
Topics: Animals; Carbon Monoxide; Cattle; Cell Line, Tumor; Female; HeLa Cells; Histidine; Humans; Interleukin-10; Interleukin-6; Mass Spectrometry; Mice; Mice, Inbred BALB C; Neoplasms; Organometallic Compounds; Prodrugs; Serum Albumin, Bovine; Tissue Distribution; Transplantation, Heterologous; Tumor Necrosis Factor-alpha | 2015 |
Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding.
Topics: Carbon Monoxide; Cystine; Cytoglobin; Ferrous Compounds; Globins; Histidine; Humans; Kinetics; Ligands; Models, Molecular; Oxidation-Reduction; Protein Binding | 2015 |
Molecular dynamics simulations indicate that tyrosineB10 limits motions of distal histidine to regulate CO binding in soybean leghemoglobin.
Topics: Carbon Monoxide; Glycine max; Histidine; Leghemoglobin; Molecular Dynamics Simulation; Oxygen; Protein Binding; Tyrosine | 2015 |
Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site.
Topics: Carbon; Carbon Monoxide; Catalytic Domain; Copper; Enzymes; Histidine; Metalloproteins; Models, Chemical; Nitrite Reductases; Oxygen; Peptides; Spectrophotometry, Infrared; Static Electricity | 2015 |
CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity.
Topics: Binding Sites; Carbon Monoxide; Circular Dichroism; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Ligands; Lysine; MicroRNAs; Models, Biological; Nitric Oxide; Protein Binding; RNA-Binding Proteins; Spectrum Analysis, Raman | 2016 |
Role of Ionic Strength and pH in Modulating Thermodynamic Profiles Associated with CO Escape from Rice Nonsymbiotic Hemoglobin 1.
Topics: Calorimetry; Carbon Monoxide; Heme; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Molecular Dynamics Simulation; Oryza; Osmolar Concentration; Plant Proteins; Protein Binding; Protein Conformation; Temperature; Thermodynamics | 2017 |
Unravelling the Non-Native Low-Spin State of the Cytochrome c-Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only.
Topics: Animals; Carbon Monoxide; Cardiolipins; Cloning, Molecular; Cytochromes c; Escherichia coli; Gene Expression; Genes, Synthetic; Histidine; Horses; Hydrogen Bonding; Methionine; Myocardium; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Unfolding; Recombinant Proteins; Temperature | 2017 |
CO-independent modification of K
Topics: Carbon Monoxide; HEK293 Cells; Histidine; Humans; Hydrogen-Ion Concentration; Organometallic Compounds; Potassium Channels | 2017 |
Direct observation of ligand migration within human hemoglobin at work.
Topics: Carbon Monoxide; Crystallography, X-Ray; Diffusion; Heme; Hemoglobins; Histidine; Humans; Ligands; Models, Molecular; Protein Conformation; Protein Subunits; Recombinant Fusion Proteins | 2020 |
A Pyrene-Triazacyclononane Anchor Affords High Operational Stability for CO
Topics: Aldehyde Oxidoreductases; Aza Compounds; Carbon Dioxide; Carbon Monoxide; Histidine; Multienzyme Complexes; Nickel; Piperidines; Pyrenes | 2022 |