heme has been researched along with lysine in 165 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 44 (26.67) | 18.7374 |
| 1990's | 34 (20.61) | 18.2507 |
| 2000's | 56 (33.94) | 29.6817 |
| 2010's | 22 (13.33) | 24.3611 |
| 2020's | 9 (5.45) | 2.80 |
| Authors | Studies |
|---|---|
| Aviram, I; Pettigrew, GW; Schejter, A | 1 |
| Hasegawa, E; Honda, K; Tsuchida, E | 3 |
| Cass, RD; Stellwagen, E | 1 |
| Morgan, WT; Muller-eberhard, U | 1 |
| Carstens, M; Neethling, AC; Percy, VA; Shanley, BC | 1 |
| Dauter, Z; Oldfield, TJ; Petratos, K; Smerdon, SJ; Wilkinson, AJ; Wilson, KS | 1 |
| Go, M; Horiuchi, T; Koga, H; Noguti, T; Tsujimura, M; Yasukochi, T; Yoshikawa, K | 1 |
| Bray, RC; Burke, JF; Sanders, SA; Smith, AT; Thorneley, RN; Veitch, NC; Williams, RJ | 1 |
| Golly, I; Hlavica, P | 1 |
| Imai, Y; Nakamura, M | 1 |
| Harris, ED; Percival, SS | 1 |
| Bernhardt, R; Ruckpaul, K; Stiel, H | 1 |
| Davis, D; Durham, B; Hall, J; Millett, F; O'Brien, P; Okamura, M; Vieira, B; Zha, XH | 1 |
| Erman, JE; Moench, SJ; Satterlee, JD | 1 |
| Ayres, M; Durham, B; Hall, J; Knaff, D; Millett, F; O'Brien, P; Zha, XH | 1 |
| Ambrosius, H | 1 |
| King, TE; Takemori, S; Yong, FC | 1 |
| Mochan, E | 1 |
| King, TE; Yong, FC | 1 |
| Stellwagen, E; Wilgus, H | 1 |
| Dose, K; Zaki, L | 1 |
| Labie, D; Wajcman, H | 1 |
| Hunter, AR; Jackson, RJ | 1 |
| Balegh, MS; Sandberg, HE | 1 |
| Hager, LP; Warme, PK | 1 |
| Schimke, RT | 1 |
| Modesto, RR; Pesce, AJ | 1 |
| Gupta, RK; Koenig, SH | 1 |
| Mazur, A | 1 |
| Nakaya, K; Shibata, K; Suzuki, T; Takenaka, O | 1 |
| Imai, K; Kotani, M; Miyaji, T; Morimoto, H; Shibata, S | 1 |
| Kadenbach, B | 1 |
| de Bruin, SH; Janssen, LH; van Os, GA | 1 |
| Bel, FR; Goodman, YE; Jackson, FL; Whitehouse, RL; Wong, PC | 1 |
| Belkhodja, O; Bierme, R; Labie, D; Rosa, J | 1 |
| Bucci, E; Fronticelli, C; Ragatz, B | 1 |
| Clark, JF; Gurd, FR; Hartzell, CR | 1 |
| Nanzyo, N; Sano, S | 1 |
| Efron, ML; Shahidi, NT | 1 |
| Bargellesi, A; Conconi, F; Pontremoli, S | 1 |
| Honig, GR; Mason, RG; Rowan, BQ | 1 |
| Borden, D; Koppenol, WH; Margoliash, E; Osheroff, N | 1 |
| Ahmed, AJ; Millett, F; Smith, HT | 1 |
| Millett, F; Stonehuerner, J; Webb, M | 1 |
| Bosshard, HR | 1 |
| Gacon, G; Kaplan, JC; Labie, D; Lostanlen, D | 1 |
| Austin, SA; Clemens, MJ | 1 |
| Garber, EA; Margoliash, E; McCracken, J; Peisach, J; Schejter, A; Theodorakis, JL | 1 |
| Bergman, LW; Ceesay, KJ; Rider, LR; Tuck, MT | 1 |
| Campos, AP; Canters, GW; Hill, HA; Hunt, NI; Teixeira, M; Ubbink, M | 1 |
| Chen, DY; Vergères, G; Waskell, L; Wu, FF | 1 |
| Barker, PD; Eltis, LD; Guillemette, JG; Inglis, SC; Mauk, AG; Miller, CM; Northrup, SH; Thomasson, KA | 1 |
| Benning, MM; Holden, HM; Meyer, TE | 1 |
| Berka, V; Chen, PF; Tsai, AL | 1 |
| Anderson, MM; Hazen, SL; Heinecke, JW; Hsu, FF | 1 |
| Johnson, RA; Kozma, F; Nasjletti, A | 1 |
| Arciero, DM; Hooper, AB | 1 |
| Futatsugi, L; Kakegawa, T; Kobayashi, H; Saito, H | 1 |
| Bandyopadhyay, D; Banerjee, RK; Das, D | 1 |
| Cole, JA; Eaves, DJ; Griffiths, I; Grove, J; James, P; Poole, RK; Staudenmann, W; White, SA | 1 |
| Hasegawa, J; Igarashi, Y; Kobayashi, Y; Kodama, T; Kyogoku, Y; Sambongi, Y; Yamazaki, K; Yamazaki, T; Yoshida, T; Yu, Y | 1 |
| Abe, N; Kadowaki, T; Nakayama, K; Okamoto, K; Ratnayake, DB; Yamamoto, K | 1 |
| Matsuura, K; Miki, K; Nagashima, KV; Osyczka, A; Shimada, K; Sogabe, S; Yoshida, M | 1 |
| da Costa, PN; LeGall, J; Messias, AC; Salgueiro, CA; Saraiva, LM; van Dongen, WM; Xavier, AV | 1 |
| Durham, B; Gennis, RB; Millett, F; Sadoski, RC; Wang, K; Zaslavsky, D | 1 |
| Matsuura, K; Nagashima, KV; Osyczka, A; Shimada, K | 1 |
| Liu, H; Mount, DB; Nasjletti, A; Wang, W | 1 |
| Buse, G; Döpner, S; Hildebrandt, P; Mauk, AG; Rosell, FI; Soulimane, T; von Walter, M | 1 |
| Fedinec, AL; Johnson, RA; Leffler, CW; Nasjletti, A; Walker, N; Yu, C | 1 |
| Daldal, F; Darrouzet, E; Knaff, DB; Li, J; Mandaci, S; Qin, H | 1 |
| Buse, G; Hellwig, P; Mäntele, W; Soulimane, T | 1 |
| Branco, LG; Colombari, E; Steiner, AA | 1 |
| Daff, S; Sagami, I; Sato, H; Shimanuki, T; Shimizu, T | 1 |
| Elliott, T; Wang, L; Wilson, S | 1 |
| Hendrich, MP; Ho, C; Ho, NT; Jeong, ST | 1 |
| Abad-Zapatero, C; Fernandez, EJ; Olsen, KW | 1 |
| Das, TK; Ferguson-Miller, S; Gennis, RB; Lee, HM; Mills, D; Rousseau, DL | 1 |
| Chen, IP; Koepke, J; Mathis, P; Michel, H | 1 |
| Branco, LG; Steiner, AA | 2 |
| Ferguson-Miller, S; Florens, L; Hiser, C; Mills, DA; Qian, J | 1 |
| Berry, EA; Chi, YI; Fernández-Velasco, JG; Huang, LS; Zhang, Z | 1 |
| Bowler, BE; Nelson, CJ | 1 |
| Kudo, T; Park, SY; Shiro, Y; Shoun, H; Takaya, N | 1 |
| Azeva, TN; Gilep, AA; Lepesheva, GI; Strushkevich, NV; Usanov, SA | 1 |
| Fedinec, AL; Johnson, RA; Leffler, CW; Nasjletti, A | 1 |
| Adelroth, P; Brändén, M; Brzezinski, P; Gennis, RB; Namslauer, A; Sigurdson, H | 1 |
| Cvrk, T; Strobel, HW | 1 |
| Boffi, A; Ceci, P; Chiancone, E; Giangiacomo, L | 1 |
| Gonzales, RJ; Walker, BR | 1 |
| de Waal, EC; Louro, RO; Turner, DL; Ubbink, M | 1 |
| Brien, JF; Hosein, S; Marks, GS; McLaughlin, BE; Nakatsu, K | 1 |
| Cheng, X; Cheranov, SY; E, S; Jaggar, JH; Leffler, CW; Tcheranova, D | 1 |
| Branco, LG; De Paula, PM; Paro, FM; Steiner, AA | 1 |
| Naik, JS; O'Donaughy, TL; Walker, BR | 1 |
| Bowler, BE; Smith, CR; Wandschneider, E | 1 |
| Naik, JS; Walker, BR | 1 |
| Mabrouk, PA; Sivakolundu, SG | 1 |
| STRYER, L | 1 |
| Hayashi, T; Ishikawa, Y; Ryu, D; Sato, H; Tomisugi, Y; Tsutsumi, H; Uno, T; Wilkinson, AJ | 1 |
| Aulakh, P; Cross, KJ; Dashper, SG; Lissel, P; Moore, C; Reynolds, EC; Slakeski, N | 1 |
| Duke, NE; Londer, YY; Long, WC; Pokkuluri, PR; Schiffer, M | 1 |
| Brunori, M; D'Itri, E; Forte, E; Giuffrè, A; Ludwig, B; Richter, OM; Sarti, P; Scandurra, FM | 1 |
| Erman, JE; Foshay, MC; Vitello, LB | 1 |
| Babcock, GT; Durham, B; Ferguson-Miller, S; Geren, L; Hiser, C; Hoganson, CW; Millett, F; Mills, DA; Qian, J; Schmidt, B; Wang, K | 1 |
| Banerjee, R; Evande, R; Ojha, S | 1 |
| Alvarez, DE; Buldain, G; de Montellano, PR; Huang, L; Lad, L; Niemevz, F; Poulos, TL; Wang, J | 1 |
| Ascoli, F; Caroppi, P; Ferri, T; Fiorucci, L; Howes, BD; Santoni, E; Santucci, R; Sinibaldi, F; Smulevich, G | 1 |
| Ferrand, M; Franc, JL; Le Fourn, V | 1 |
| De la Rosa, MA; Díaz-Moreno, I; Díaz-Quintana, A; Hansson, O; Karlsson, BG; Molina-Heredia, FP; Nieto, PM | 1 |
| Bertero, MG; Blasco, F; Boroumand, N; Ginet, N; Palak, M; Rothery, RA; Strynadka, NC; Weiner, JH | 1 |
| Allen, JW; Ferguson, SJ; Leach, N | 1 |
| Albrecht, T; Haehnel, W; Hildebrandt, P; Li, W; Ulstrup, J | 1 |
| Canters, GW; Ubbink, M; van Roon, AM; Worrall, JA | 1 |
| Jellen, EE; Ryzhov, V | 1 |
| Durham, B; Ferguson-Miller, S; Geren, L; Hiser, C; Millett, F; Mills, DA; Schmidt, B | 1 |
| Cukier, RI; Ferguson-Miller, S; Mills, DA; Seibold, SA | 1 |
| Shamloul, R; Wang, R | 1 |
| Evans, JP; La Mar, GN; Ogura, H; Ortiz de Montellano, PR; Wang, J | 1 |
| Almeida, MC; Branco, LG; Ravanelli, MI | 1 |
| Chan, AC; I Rosell, F; Lelj-Garolla, B; Mauk, AG; Murphy, ME; Pedersen, KA | 1 |
| Branco, LG; Nascimento, CG | 2 |
| Kozak, W; Szefer, M; Terlecki, P; Walentynowicz, K; Wojtal, B; Wrotek, S | 1 |
| Christensen, O; Ferguson, SJ; Harvat, EM; Stevens, JM; Thöny-Meyer, L | 1 |
| Bertrand, P; Grimaldi, S; Guigliarelli, B; Lanciano, P; Magalon, A | 1 |
| Elmore, BO; Ferrara, JD; Hooper, AB; Pearson, AR; Wilmot, CM; Yang, C | 1 |
| Baddam, S; Bandi, S; Bowler, BE | 1 |
| Bröcker, MJ; Ganskow, S; Heathcote, P; Heinz, DW; Jahn, D; Moser, J; Schubert, WD; Virus, S | 1 |
| Branco, LG; Ravanelli, MI | 1 |
| Bogel, G; Groves, MR; Ortiz de Orué Lucana, D; Zou, P | 1 |
| Bumke, MA; ElSohly, MA; Galal, AM; Gul, W; Han, B; Hollingshead, MG; Newton, DL; Slade, D; Stockwin, LH; Yu, SX | 1 |
| Wang, XB; Wei, WL | 1 |
| De La Rosa, MÁ; Díaz-Moreno, I; García-Heredia, JM; Hildebrandt, P; Ly, HK; Utesch, T | 1 |
| Dantas, JM; Londer, YY; Morgado, L; Pokkuluri, PR; Salgueiro, CA; Simões, T | 1 |
| Clapp, KM; Ford, MJ; Jenkins, GJ; Lau, M; Morishima, Y; Osawa, Y; Peng, HM | 1 |
| Abu Tarboush, N; Davidson, VL; Geng, J; Liu, A; Shin, S | 1 |
| Bowler, BE; Khan, MK | 1 |
| Hase, T; Hori, H; Nakanishi, N; Park, SY; Rahman, MM; Sakamoto, Y; Tsubaki, M | 1 |
| Bowler, BE; Cherney, MM; Junior, CC | 1 |
| Brown, JM; Gilevicius, L; Johnson, EA; Lecomte, JT; Nye, DB; Preimesberger, MR; Rice, SL; Wenke, BB; Witman, GB | 1 |
| Branco, LG; Carvalho-Costa, PG; Leite-Panissi, CR | 1 |
| Goodwin, DC; Huang, J; Panizzi, JR; Panizzi, P; Smith, F | 1 |
| Alden, SL; Amacher, JF; Hoke, KR; Lisi, GP; Madden, DR; Pletneva, EV; Zhong, F; Zhu, MQ | 1 |
| Bosch, J; Boucher, LE; Lecomte, JT; Preimesberger, MR; Rice, SL; Schlessman, JL | 1 |
| Chelstowska, A; Jastrzebska, Z; Kaminska, J; Plochocka, D; Rytka, J; Sadurska, A; Zoladek, T | 1 |
| Borek, A; Cieluch, E; Kuleta, P; Osyczka, A; Pintscher, S; Sarewicz, M | 1 |
| Barr, I; Burstyn, JN; Guo, F; Hines, JP; Jacob, JP; Lukat-Rodgers, GS; Rodgers, KR; Smith, AT | 1 |
| Gu, J; Pletneva, EV; Shin, DW | 1 |
| Azami-Movahed, M; Ebrahim-Habibi, A; Ghasemi, A; Meratan, AA; Nemat-Gorgani, M | 1 |
| Lecomte, JTJ; Majumdar, A; Nye, DB; Preimesberger, MR | 1 |
| Davidson, VL | 1 |
| Johnson, EA; Lecomte, JTJ; Nye, DB; Russo, MM; Schlessman, JL | 1 |
| Johnson, EA; Lecomte, JTJ; Mai, MH; Nye, DB | 1 |
| Dojun, N; Ishimori, K; Muranishi, K; Uchida, T | 1 |
| Deniz, E; Heit, S; Klein, M; Lancaster, CRD; Mäntele, W; Wille, G | 1 |
| Feng, C; Li, J; Zheng, H | 1 |
| Coleman, RE; Lancaster, KM | 1 |
| Esackimuthu, P; Saraswathi, NT | 1 |
| Alepuz, P; Barba-Aliaga, M; Corman, A; Martínez-Pastor, MT; Stanciu, A; Villarroel-Vicente, C | 1 |
| Capece, L; Estrin, DA; Julió Plana, L; Lecomte, JTJ; Martinez Grundman, JE; Schlessman, JL | 1 |
| Banerjee, S | 1 |
| Boal, AK; Bollinger, JM; Chang, MCY; Krebs, C; McBride, MJ; Nair, MA; Neugebauer, ME; Sil, D; Slater, JW | 1 |
2 review(s) available for heme and lysine
| Article | Year |
|---|---|
Where is 'outside' in cytochrome c oxidase and how and when do protons get there?
Topics: Aspartic Acid; Binding Sites; Electron Transport Complex IV; Heme; Lysine; Models, Molecular; Mutation; Oxidation-Reduction; Propionates; Proton Pumps; Proton-Motive Force; Protons; Rhodobacter sphaeroides | 2000 |
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 |
163 other study(ies) available for heme and lysine
| Article | Year |
|---|---|
The role of the lysines in the alkaline heme-linked ionization of ferric cytochrome c.
Topics: Amidines; Animals; Binding Sites; Cytochrome c Group; Heme; Horses; Hydrogen-Ion Concentration; Lysine; Maleates; Protein Binding; Protein Conformation; Spectrophotometry; Spectrophotometry, Ultraviolet | 1976 |
Cooperative reactions of poly-L-lysine-heme complex with molecular oxygen, carbon monoxide, or cyanide ion.
Topics: Binding Sites; Calorimetry; Carbon Monoxide; Circular Dichroism; Cyanides; Heme; Hydrogen-Ion Concentration; Kinetics; Lysine; Oxygen; Partial Pressure; Peptides; Protein Binding; Protein Conformation; Spectrophotometry; Thermodynamics | 1976 |
Complexation of iron hexacyanides by cytochrome c. Evidence for electron exchange at the exposed heme edge.
Topics: Animals; Binding Sites; Cytochrome c Group; Electron Transport; Ferricyanides; Ferrocyanides; Heme; Horses; Hydrogen-Ion Concentration; Ligands; Lysine; Methionine; Myocardium; Osmolar Concentration; Protein Binding | 1975 |
Chemical modification of histidine residues of rabbit hemopexin.
Topics: Acetates; Animals; Apoproteins; Arginine; Binding Sites; Heme; Hemopexin; Histidine; Kinetics; Lysine; Porphyrins; Protein Binding; Protein Conformation; Rabbits; Spectrophotometry; Spectrophotometry, Ultraviolet | 1976 |
Neurochemical aspects of porphyria. Studies on the possible neurotoxicity of delta-aminolaevulinic acid.
Topics: Aminolevulinic Acid; Animals; Behavior, Animal; Brain; Carbon Radioisotopes; Cerebral Ventricles; Female; Heme; Injections; Levulinic Acids; Liver; Lysine; Methionine; Nephrectomy; Nerve Tissue Proteins; Rats; Sulfur Radioisotopes | 1975 |
Complexes between synthetic polymer ligands and ferri-delta and ferro-protoporphyrin IX.
Topics: Allosteric Site; Amines; Benzyl Compounds; Circular Dichroism; Dose-Response Relationship, Drug; Ferric Compounds; Ferrous Compounds; Glutamates; Heme; Imidazoles; Iron; Ligands; Lysine; Optical Rotatory Dispersion; Oxygen; Polymers; Porphyrins; Protein Conformation; Protoporphyrins; Spectrum Analysis; Thermodynamics; Viscosity | 1975 |
Reaction of polymer-heme complexes with carbon monoxide or molecular oxygen.
Topics: Binding Sites; Carbon Monoxide; Heme; Kinetics; Lysine; Oxygen; Peptides; Polyethylenes; Povidone; Protein Binding | 1975 |
High-resolution X-ray structures of pig metmyoglobin and two CD3 mutants: Mb(Lys45----Arg) and Mb(Lys45----Ser).
Topics: Animals; Arginine; Binding Sites; Crystallography; Fourier Analysis; Heme; Iron; Ligands; Lysine; Metmyoglobin; Mutation; Protein Conformation; Serine; Structure-Activity Relationship; Swine; X-Ray Diffraction | 1992 |
Hydrogen bond network of cytochrome P-450cam: a network connecting the heme group with helix K.
Topics: Arginine; Cytochrome P-450 Enzyme System; Heme; Hydrogen Bonding; Lysine; Models, Molecular; Mutation; Protein Conformation | 1992 |
Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys.
Topics: Arginine; Cyanides; Heme; Horseradish Peroxidase; Hydroxamic Acids; Isoenzymes; Lysine; Magnetic Resonance Spectroscopy; Phenylalanine; Protein Conformation; Recombinant Proteins; Structure-Activity Relationship; Valine | 1992 |
Chemical modification of lysine residues in cytochrome P450LM2 (P450IIB4): influence on heme liganding of arylamines.
Topics: Amines; Animals; Aryl Hydrocarbon Hydroxylases; Cytochrome P-450 Enzyme System; Heme; Heterocyclic Compounds; Lysine; Male; Protein Binding; Protein Conformation; Protein Denaturation; Rabbits; Steroid Hydroxylases; Structure-Activity Relationship | 1992 |
Nitrogenous ligation at the sixth coordination position of the Thr-301 to Lys-mutated P450IIC2 heme iron.
Topics: Base Sequence; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System; DNA Probes; Heme; Iron; Ligands; Lysine; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrogen; Oxidation-Reduction; Saccharomyces cerevisiae; Spectrophotometry; Threonine | 1991 |
Regulation of Cu,Zn superoxide dismutase with copper. Caeruloplasmin maintains levels of functional enzyme activity during differentiation of K562 cells.
Topics: Biological Transport; Cell Differentiation; Cell Line; Ceruloplasmin; Copper; DNA Replication; Heme; Humans; Kinetics; Leukemia, Erythroblastic, Acute; Lysine; Neoplasm Proteins; Subcellular Fractions; Superoxide Dismutase | 1991 |
Distance between lysine 384 and heme of cytochrome P-450 LM2 (P-450 IIB4) studied by fluorescence energy transfer measurements.
Topics: Animals; Binding Sites; Cytochrome P-450 Enzyme System; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Dyes; Heme; Lysine; Male; Microsomes, Liver; Phenobarbital; Protein Conformation; Rabbits; Spectrometry, Fluorescence; Thiocyanates | 1989 |
Reaction of cytochromes c and c2 with the Rhodobacter sphaeroides reaction center involves the heme crevice domain.
Topics: Amino Acid Sequence; Animals; Bacterial Proteins; Binding Sites; Cytochrome c Group; Cytochromes c2; Heme; Horses; Kinetics; Lasers; Lysine; Photosynthetic Reaction Center Complex Proteins; Protein Binding; Protein Conformation; Rhodobacter sphaeroides | 1987 |
A proton NMR study of the non-covalent complex of horse cytochrome c and yeast cytochrome-c peroxidase and its comparison with other interacting protein complexes.
Topics: Animals; Computer Graphics; Cytochrome c Group; Cytochrome-c Peroxidase; Heme; Horses; Lysine; Magnetic Resonance Spectroscopy; Models, Molecular; Peroxidases; Protein Binding; Protein Conformation; Saccharomyces cerevisiae | 1987 |
The reaction of cytochromes c and c2 with the Rhodospirillum rubrum reaction center involves the heme crevice domain.
Topics: Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Cytochrome c Group; Cytochromes c2; Electrochemistry; Heme; Kinetics; Lysine; Nitrobenzoates; Oxidation-Reduction; Photochemistry; Rhodospirillum rubrum; Spectrophotometry | 1987 |
[Regulation of antibody affinity].
Topics: Adsorption; Animals; Antibodies; Antibody Specificity; Binding Sites, Antibody; Brucella abortus; Carps; Cattle; Dansyl Compounds; Dinitrophenols; gamma-Globulins; Heme; Hemocyanins; Humans; Immunoglobulin G; Immunoglobulin M; Immunologic Techniques; Lysine; Precipitin Tests; Rabbits; Serum Albumin; Tritium; Turtles | 1973 |
Interaction of heme A and polylysine.
Topics: Borates; Chemical Phenomena; Chemistry; Electron Transport Complex IV; Heme; Lysine; Peptides | 1966 |
The nature of complex formation between cytochrome c and cytochrome c peroxidase.
Topics: Acetates; Binding Sites; Chromatography, Gel; Cytochromes; Electron Transport Complex IV; Esters; Guanidines; Heme; Kinetics; Lysine; Molecular Weight; Peptides; Peroxidases; Protamines; Proteins; Saccharomyces | 1970 |
Optical rotatory dispersion of alkali-denatured cytochrome oxidase and heme alpha-polylysine complexes.
Topics: Electron Transport Complex IV; Heme; Lysine; Optical Rotatory Dispersion; Peptides | 1971 |
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Topics: Animals; Cytochrome c Group; Guanidines; Heme; Horses; Hydrogen-Ion Concentration; In Vitro Techniques; Iron; Ligands; Lysine; Methionine; Myocardium; Spectrophotometry, Ultraviolet | 1974 |
[The peroxidatic and catalatic activity of hemoproteinoids].
Topics: Amino Acids; Blood Proteins; Catalysis; Heme; Hydrogen-Ion Concentration; Lysine; Molecular Weight; Oxidation-Reduction | 1971 |
Functional disorders of some haemoglobins mutated in the haem pocket.
Topics: Anemia, Hemolytic; Diphosphoglyceric Acids; Erythrocytes; Glutamates; Heinz Bodies; Heme; Hemoglobins, Abnormal; Humans; Lysine; Mutation; Splenomegaly; Structure-Activity Relationship | 1974 |
Control of haemoglobin synthesis: coordination of alpha and beta chain synthesis.
Topics: Animals; Carbon Radioisotopes; Chromatography, Gel; Cycloheximide; Globins; Heme; Hemoglobins; Humans; Iron; Lysine; Peptide Chain Initiation, Translational; Peptide Fragments; Puromycin; Rabbits; Reticulocytes; Thalassemia; Tritium | 1972 |
Evidence for the coordination of a histidyl residue to heme. I. Far ultraviolet spectral studies of model complexes.
Topics: Animals; Buffers; Catalase; Chemical Phenomena; Chemistry; Cyanides; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Imidazoles; Iron; Lysine; Methemoglobin; Models, Chemical; Myoglobin; Peptides; Peroxidases; Spectrophotometry, Ultraviolet | 1973 |
Affinity labeling of myoglobin with mesoheme sulfuric anhydride.
Topics: Amino Acids; Anhydrides; Animals; Chemical Phenomena; Chemistry; Chromatography, Thin Layer; Heme; Horses; Indicators and Reagents; Lysine; Myoglobin; Pepsin A; Peptides; Spectrophotometry; Sulfuric Acids; X-Ray Diffraction | 1970 |
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 |
The reaction of 4,4'-difluoro-3,3'-dinitro-diphenyl sulfone with gamma-globulin and horseradish peroxidase.
Topics: Animals; Antibodies; Chemical Phenomena; Chemistry; Chromatography, Gel; Dialysis; Goats; Heme; Humans; Immunoglobulin G; Lysine; Methods; Peroxidases; Plants; Polymers; Protein Binding; Rabbits; Sulfones; Temperature; Time Factors | 1971 |
Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C.
Topics: Animals; Chemical Phenomena; Chemistry; Cytochromes; Electron Transport; Heme; Horses; Hydrogen-Ion Concentration; Iron; Lysine; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Protons; Temperature; Threonine; Water | 1971 |
Role of the spleen in iron metabolism.
Topics: Animals; Bone Marrow; Carbon Isotopes; Cobalt; Enzymes; Erythrocytes; Erythropoietin; Glycine; Heme; Hemorrhage; Histones; Iron; Iron Isotopes; Liver; Lyases; Lymphoma, Non-Hodgkin; Lysine; Phenylhydrazines; Porphyrins; Radiation Effects; Rats; Reticulocytes; Spleen | 1969 |
States of amino acid residues in proteins. XIX. Modification of arginine residues in myoglobin.
Topics: Acrylates; Aldehydes; Animals; Arginine; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Cyanides; Dextrans; Electrophoresis; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iodoacetates; Lysine; Methemoglobin; Methods; Methylcellulose; Myocardium; Myoglobin; Spectrophotometry; Time Factors; Ultracentrifugation; Urea | 1969 |
Studies on the function of abnormal hemoglobins. II. Oxygen equilibrium of abnormal hemoglobins: Shimonoseki, Ube II, Hikari, Gifu, and Agenogi.
Topics: Heme; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Japan; Lysine; Methemoglobin; Oxygen; Spectrophotometry; Temperature | 1970 |
Biosynthesis of cytochrome c. The sites of synthesis of apoprotein and holoenzyme.
Topics: Amino Acids; Animals; Carbon Isotopes; Chromatography, Ion Exchange; Cytochromes; Endoplasmic Reticulum; Heme; Iron Isotopes; Kinetics; Levulinic Acids; Lysine; Male; Microsomes, Liver; Mitochondria, Liver; Protein Biosynthesis; Rats | 1970 |
H+ titration studies on human hemoglobin.
Topics: Arginine; Benzoates; Chemical Phenomena; Chemistry; Globins; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Iodoacetates; Lysine; Mathematics; Mercury; Organometallic Compounds; Oxygen; Sulfhydryl Compounds | 1970 |
Taxonomic status of facultative and strictly anaerobic "corroding bacilli" that have been classified as Bacteroides corrodens.
Topics: Anaerobiosis; Bacteroides; Carboxy-Lyases; Caseins; Catalase; Cell Movement; Cystine; Cytosine Nucleotides; Fermentation; Gelatin; Guanine Nucleotides; Heme; Humans; Hydrolysis; Indoles; Lysine; Microscopy, Electron; Nitrates; Oxidation-Reduction; Oxidoreductases; Peptide Hydrolases; Urease | 1971 |
Hemoglobin toulouse alpha 2 beta 2 66 (E 10) LysGlu. Structure and consequences in molecular pathology.
Topics: Alkylation; Benzoates; Chemical Phenomena; Chemistry; Chemistry, Physical; Chromatography, Gel; Dialysis; Drug Stability; Fetal Hemoglobin; France; Globins; Glutamates; Heme; Hemoglobins, Abnormal; Hot Temperature; Humans; Iron Isotopes; Lysine; Mercury; Methemoglobin; Organometallic Compounds; Oxidation-Reduction; Oxygen; Protein Denaturation; Sulfhydryl Compounds | 1971 |
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 |
Hemic acid dissociation in whale, seal, and porpoise myoglobins and their alkylated derivatives.
Topics: Alkylation; Animals; Caniformia; Cetacea; Chemical Phenomena; Chemistry; Dolphins; Heme; Histidine; Hydrogen-Ion Concentration; Lysine; Myoglobin; Physiology, Comparative | 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 |
Excretion of delta-aminolevulinic acid in the absence of demonstrable erythropoiesis.
Topics: Adolescent; Amino Acids; Aminobutyrates; Ammonia; Anemia, Aplastic; Autoanalysis; Chemistry, Clinical; Child; Child, Preschool; Chromatography, Ion Exchange; Erythropoiesis; Heme; Histidine; Humans; Lead Poisoning; Levulinic Acids; Lysine; Middle Aged; Ornithine; Phenylalanine; Tyrosine | 1968 |
Excess of alpha-globin synthesis in homozygous beta-thalassemia. Its cytoplasmic molecular forms.
Topics: Adult; Blood Proteins; Centrifugation, Density Gradient; Child; Child, Preschool; Chromatography, Ion Exchange; Cytoplasm; Erythrocytes; Globins; Heme; Hemoglobins; Hemolysis; Homozygote; Humans; Infant, Newborn; Infant, Premature; Leucine; Lysine; Peptides; Thalassemia; Tritium; Valine | 1968 |
Unequal synthesis of complementary globin chains of human fetal hemoglobin by the effect of L-O-methylthreonine.
Topics: Blood Proteins; Carbon Isotopes; Chromatography, Gel; Complement System Proteins; Depression, Chemical; Erythroblastosis, Fetal; Female; Fetal Hemoglobin; Globins; Heme; Hemolysis; Humans; In Vitro Techniques; Infant, Newborn; Isoleucine; Leucine; Lysine; Peptide Biosynthesis; Pregnancy; Solubility; Thalassemia; Threonine | 1969 |
Electrostatic interactions in cytochrome c. The role of interactions between residues 13 and 90 and residues 79 and 47 in stabilizing the heme crevice structure.
Topics: Animals; Computers; Cytochrome c Group; Dinitrophenols; Drug Stability; Haplorhini; Heme; Horses; Humans; Hydrogen-Ion Concentration; Lysine; Models, Molecular; Myocardium; Protein Binding; Protein Conformation; Species Specificity; Spectrophotometry; Trinitrobenzenes | 1980 |
Electrostatic interaction of cytochrome c with cytochrome c1 and cytochrome oxidase.
Topics: Animals; Calorimetry; Cytochrome c Group; Cytochromes c1; Electron Transport Complex IV; Heme; Horses; Kinetics; Lysine; Myocardium; Osmolar Concentration; Polarography; Submitochondrial Particles; Succinate Cytochrome c Oxidoreductase | 1981 |
The use of specific lysine modifications to locate the reaction site of cytochrome c with sulfite oxidase.
Topics: Binding Sites; Cytochrome c Group; Heme; Lysine; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Structure-Activity Relationship | 1980 |
Alkaline isomerization of ferricytochrome c: lysine is not replacing methionine at the sixth co-ordination site of the haem iron.
Topics: Acetylation; Amino Acids; Animals; Binding, Competitive; Cytochrome c Group; Heme; Hydrogen-Ion Concentration; Isomerism; Kinetics; Lysine; Methionine; Phenylalanine; Protein Conformation | 1981 |
Interaction between cytochrome b5 and hemoglobin: involvement of beta 66 (E10) and beta 95 (FG2) lysyl residues of hemoglobin.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cytochromes; Heme; Hemoglobins, Abnormal; Humans; Kinetics; Lysine; Methemoglobin; Oxidation-Reduction; Protein Binding; Protein Conformation; Rabbits; Structure-Activity Relationship | 1980 |
The effects of haem on translational control of protein synthesis in cell-free extracts from fed and lysine-derived Ehrlich ascites tumour cells.
Topics: Animals; Carcinoma, Ehrlich Tumor; Heme; Kinetics; Lysine; Mice; Neoplasm Proteins; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Phosphorylation; Protein Biosynthesis; Reticulocytes | 1981 |
A chemical modification of cytochrome-c lysines leading to changes in heme iron ligation.
Topics: Animals; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Iron; Lysine; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Spectrophotometry; Sulfhydryl Compounds; Tetramethylphenylenediamine | 1995 |
The relationship between the trimethylation of lysine 77 and cytochrome c metabolism in Saccharomyces cerevisiae.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome c Group; DNA Restriction Enzymes; Drug Stability; Gene Transfer Techniques; Heme; Lysine; Methylation; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids; Saccharomyces cerevisiae | 1994 |
Characterization of mutant Met100Lys of cytochrome c-550 from Thiobacillus versutus with lysine-histidine heme ligation.
Topics: Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutation; Spectrophotometry; Structure-Activity Relationship; Thiobacillus | 1994 |
The function of tyrosine 74 of cytochrome b5.
Topics: Animals; Cytochromes b5; Heme; Hot Temperature; In Vitro Techniques; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Rats; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Tyrosine; Urea | 1993 |
Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochrome c Group; Cytochromes b5; Cytochromes c; Heme; Histidine; Kinetics; Liver; Lysine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1993 |
Molecular structure of a high potential cytochrome c2 isolated from Rhodopila globiformis.
Topics: Amino Acid Sequence; Bacteria; Crystallization; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c2; Glycine; Heme; Hydrogen Bonding; Least-Squares Analysis; Lysine; Models, Molecular; Protein Structure, Secondary; Water | 1996 |
Spatial relationship between L-arginine and heme binding sites of endothelial nitric-oxide synthase.
Topics: Arginine; Binding Sites; Binding, Competitive; Cyanides; Endothelium, Vascular; Heme; Humans; Imidazoles; Kinetics; Lysine; Nitric Oxide Synthase | 1996 |
Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. A mechanism for the generation of highly reactive alpha-hydroxy and alpha,beta-unsaturated
Topics: Acetaldehyde; Acrolein; Aldehydes; Amino Acids; Catalase; Chlorides; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Heme; Humans; Hydrogen Peroxide; Hydroxy Acids; Hypochlorous Acid; Inflammation; Lysine; Mass Spectrometry; Molecular Structure; Neutrophil Activation; Neutrophils; Oxidation-Reduction; Peroxidase; Serine; Threonine | 1997 |
Role of carbon monoxide in heme-induced vasodilation.
Topics: Animals; Arterioles; Carbon Monoxide; Heme; Lysine; Male; Muscle, Smooth, Vascular; Rats; Rats, Sprague-Dawley; Vasodilation | 1997 |
Evidence for a crosslink between c-heme and a lysine residue in cytochrome P460 of Nitrosomonas europaea.
Topics: Chromatography, Gel; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Cytochromes; Heme; Lysine; Nitrosomonas | 1997 |
Growth of an Escherichia coli mutant deficient in respiration.
Topics: Aerobiosis; Culture Media; Escherichia coli; Genes, Bacterial; Heme; Hydrogen-Ion Concentration; Lysine; Mutation; Oxygen Consumption; Proton-Motive Force | 1997 |
Oxidative inactivation of gastric peroxidase by site-specific generation of hydroxyl radical and its role in stress-induced gastric ulceration.
Topics: Animals; Ascorbic Acid; Cold Temperature; Copper; Free Radical Scavengers; Gastric Mucosa; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Hydroxyl Radical; Lysine; Oxidation-Reduction; Peroxidase; Rats; Rats, Wistar; Reactive Oxygen Species; Restraint, Physical; Stomach Ulcer; Stress, Physiological | 1998 |
Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli.
Topics: Anaerobiosis; Chromatography, High Pressure Liquid; Cysteine; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Gene Deletion; Genes, Bacterial; Heme; Lysine; Mass Spectrometry; Mutagenesis, Site-Directed; Mutation; Nitrite Reductases; Operon; Oxidation-Reduction; Plasmids | 1998 |
Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy.
Topics: Amino Acid Sequence; Arginine; Bacteria, Aerobic; Bacterial Proteins; Crystallography, X-Ray; Cytochrome c Group; Heme; Hydrogen Bonding; Lysine; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptides; Protein Conformation; Protein Folding; Protons; Pseudomonas aeruginosa; Sequence Homology, Amino Acid; Solutions; Thermodynamics; Tyrosine | 1998 |
Involvement of a lysine-specific cysteine proteinase in hemoglobin adsorption and heme accumulation by Porphyromonas gingivalis.
Topics: Adhesins, Bacterial; Adsorption; Base Sequence; Cysteine Endopeptidases; DNA Probes; DNA, Bacterial; Fibrinogen; Gingipain Cysteine Endopeptidases; Hemagglutination Tests; Hemagglutinins; Heme; Hemoglobins; Hydrolysis; Lysine; Mutation; Porphyromonas gingivalis; Receptors, Cell Surface | 1998 |
Interaction site for soluble cytochromes on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center mapped by site-directed mutagenesis.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Cytochromes; Cytochromes c; Electron Transport; Glutamic Acid; Heme; Light-Harvesting Protein Complexes; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Photosynthetic Reaction Center Complex Proteins; Protein Binding; Rhodospirillaceae; Solubility; Spectrophotometry; Static Electricity | 1998 |
Replacement of lysine 45 by uncharged residues modulates the redox-Bohr effect in tetraheme cytochrome c3 of Desulfovibrio vulgaris (Hildenborough).
Topics: Amino Acid Substitution; Cytochrome c Group; Desulfovibrio vulgaris; Electron Transport; Heme; Lysine; Magnetic Resonance Spectroscopy; Models, Molecular; Oxidation-Reduction; Protein Conformation; Spectrophotometry; Thermodynamics | 1998 |
Single electron reduction of cytochrome c oxidase compound F: resolution of partial steps by transient spectroscopy.
Topics: 2,2'-Dipyridyl; Animals; Cattle; Coordination Complexes; Electron Transport; Electron Transport Complex IV; Heme; Indicators and Reagents; Kinetics; Lysine; Methionine; Oxidation-Reduction; Photolysis; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry | 1998 |
Interaction site for high-potential iron-sulfur protein on the tetraheme cytochrome subunit bound to the photosynthetic reaction center of Rubrivivax gelatinosus.
Topics: Bacterial Proteins; Binding Sites; Cytochromes; Electron Transport; Glutamic Acid; Heme; Iron-Sulfur Proteins; Light-Harvesting Protein Complexes; Lysine; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Photosynthetic Reaction Center Complex Proteins; Rhodospirillaceae; Valine | 1999 |
Carbon monoxide stimulates the apical 70-pS K+ channel of the rat thick ascending limb.
Topics: Animals; Biliverdine; Carbon Monoxide; Enzyme Inhibitors; Female; Gene Expression Regulation, Enzymologic; Heme; Heme Oxygenase (Decyclizing); Kidney; Lysine; Male; NADP; Patch-Clamp Techniques; Porphyrins; Potassium Channels; Rats; Rats, Sprague-Dawley; RNA | 1999 |
The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase.
Topics: Alanine; Animals; Binding Sites; Cattle; Cytochrome c Group; Electron Transport; Electron Transport Complex IV; Heme; Kinetics; Lysine; Models, Molecular; Mutation; Phospholipids; Polylysine; Protein Conformation; Spectrum Analysis, Raman | 1999 |
Carbon monoxide and cerebral microvascular tone in newborn pigs.
Topics: Animals; Animals, Newborn; Brain; Brain Chemistry; Carbon Monoxide; Cerebral Arteries; Cerebrovascular Circulation; Chromium; Cyclic AMP; Cyclic GMP; Dose-Response Relationship, Drug; Heme; Heme Oxygenase (Decyclizing); Lysine; Mesoporphyrins; Microcirculation; Nitroarginine; Pia Mater; Potassium Channels; Swine; Tetraethylammonium; Vasodilation; Vasodilator Agents | 1999 |
Substitution of the sixth axial ligand of Rhodobacter capsulatus cytochrome c1 heme yields novel cytochrome c1 variants with unusual properties.
Topics: Amino Acid Substitution; Binding Sites; Cytochromes c1; Electron Transport Complex III; Heme; Histidine; Ligands; Lysine; Methionine; Mutagenesis, Site-Directed; NADH Dehydrogenase; Oxidation-Reduction; Rhodobacter capsulatus; Spectrophotometry | 1999 |
Electrochemical, FTIR, and UV/VIS spectroscopic properties of the ba(3) oxidase from Thermus thermophilus.
Topics: Arginine; Aspartic Acid; Buffers; Cytochrome b Group; Deuterium Oxide; Electrochemistry; Electron Transport Complex IV; Glutamic Acid; Heme; Lysine; Oxidation-Reduction; Peptides; Phosphates; Porphyrins; Potentiometry; Propionates; Protein Conformation; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Thermus thermophilus; Tyrosine; Water | 1999 |
Carbon monoxide as a novel mediator of the febrile response in the central nervous system.
Topics: Animals; Body Temperature; Carbon Monoxide; Central Nervous System; Deuteroporphyrins; Enzyme Inhibitors; Fever; Heme; Heme Oxygenase (Decyclizing); Injections, Intraperitoneal; Injections, Intraventricular; Lipopolysaccharides; Lysine; Male; Rats; Rats, Wistar; Reference Values; Sodium Chloride; Time Factors | 1999 |
Crucial role of Lys(423) in the electron transfer of neuronal nitric-oxide synthase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Catalysis; Cattle; Crystallography, X-Ray; Electron Transport; Heme; Kinetics; Lysine; Models, Molecular; Molecular Sequence Data; Nerve Tissue Proteins; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Potassium Chloride; Protein Conformation; Spectrophotometry, Atomic | 1999 |
A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium.
Topics: Adenosine Triphosphatases; Aldehyde Oxidoreductases; Amino Acid Sequence; ATP-Dependent Proteases; Base Sequence; Chromosomes, Bacterial; Endopeptidase Clp; Enzyme Stability; Escherichia coli; Escherichia coli Proteins; Feedback; Gene Expression; Gene Expression Regulation, Bacterial; Genetic Complementation Test; Heat-Shock Proteins; Heme; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids; Protease La; Recombinant Proteins; RNA, Transfer, Glu; Salmonella typhimurium; Serine Endopeptidases | 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 |
Crystal structure of Lysbeta(1)82-Lysbeta(2)82 crosslinked hemoglobin: a possible allosteric intermediate.
Topics: Allosteric Regulation; Amino Acid Sequence; Aspirin; Binding Sites; Cross-Linking Reagents; Crystallization; Crystallography, X-Ray; Dimerization; Heme; Hemoglobins; Humans; Lysine; Models, Molecular; Molecular Sequence Data; Oxygen; Oxyhemoglobins; Protein Structure, Tertiary; Thermodynamics | 2000 |
Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Cattle; Electron Transport Complex IV; Enzyme Activation; Glutamine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Proton Pumps; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tyrosine | 2000 |
Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis.
Topics: Amino Acid Substitution; Cysteine; Cytochrome c Group; Electron Transport; Heme; Kinetics; Lysine; Mutagenesis, Site-Directed; Oxidation-Reduction; Photosynthetic Reaction Center Complex Proteins; Plasmids; Rhodopseudomonas; Spectrophotometry | 2000 |
Central CO-heme oxygenase pathway raises body temperature by a prostaglandin-independent way.
Topics: Animals; Body Temperature; Carbon Monoxide; Central Nervous System; Cyclooxygenase Inhibitors; Deuteroporphyrins; Dinoprostone; Enzyme Inhibitors; Fever; Heme; Heme Oxygenase (Decyclizing); Indomethacin; Injections, Intraperitoneal; Injections, Intraventricular; Lipopolysaccharides; Lysine; Male; Prostaglandins; Rats; Rats, Wistar; Time Factors | 2000 |
X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii.
Topics: Amino Acid Sequence; Animals; Chlamydomonas reinhardtii; Crystallography, X-Ray; Cytochromes; Cytochromes f; Dimerization; Heme; Lysine; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid | 2000 |
pH dependence of formation of a partially unfolded state of a Lys 73 --> His variant of iso-1-cytochrome c: implications for the alkaline conformational transition of cytochrome c.
Topics: Amino Acid Substitution; Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Lysine; Models, Chemical; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Folding; Saccharomyces cerevisiae; Titrimetry | 2000 |
A positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH.
Topics: Amino Acid Sequence; Arginine; Binding Sites; Bromides; Camphor 5-Monooxygenase; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Heme; Kinetics; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Nitric Oxide; Oxidoreductases; Phosphates; Protein Structure, Secondary; Sequence Homology, Amino Acid; Spectrophotometry | 2001 |
Site-directed mutagenesis of cytochrome P450scc (CYP11A1). Effect of lysine residue substitution on its structural and functional properties.
Topics: Adrenodoxin; Amino Acid Sequence; Animals; Cholesterol Side-Chain Cleavage Enzyme; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Glutamic Acid; Heme; Humans; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Protein Folding; Sequence Homology, Amino Acid; Spectrophotometry; Thermodynamics; Time Factors | 2000 |
Contributions of prostacyclin and nitric oxide to carbon monoxide-induced cerebrovascular dilation in piglets.
Topics: Animals; Animals, Newborn; Arterioles; Carbon Monoxide; Heme; Indomethacin; Kinetics; Lysine; Microcirculation; Muscle, Smooth, Vascular; Nitric Oxide; Nitroarginine; Peptides; Pia Mater; Potassium Channels; Scorpion Venoms; Swine; Tetraethylammonium; Vasodilation; Vasodilator Agents | 2001 |
On the role of the K-proton transfer pathway in cytochrome c oxidase.
Topics: Amino Acid Substitution; Binding Sites; Biological Transport; Electron Transport; Electron Transport Complex IV; Electrons; Heme; Hydrogen Bonding; Lysine; Models, Molecular; Mutation; Oxygen; Photolysis; Protein Conformation; Protons; Rhodobacter sphaeroides; Spectrum Analysis; Static Electricity | 2001 |
Role of LYS271 and LYS279 residues in the interaction of cytochrome P4501A1 with NADPH-cytochrome P450 reductase.
Topics: Amino Acid Substitution; Benzene Derivatives; Binding Sites; Circular Dichroism; Coumarins; Cytochrome P-450 CYP1A1; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Iron; Kinetics; Lysine; Mutation; NADPH-Ferrihemoprotein Reductase; Oxazines; Protein Binding; Protein Structure, Secondary | 2001 |
The mutation K30D disrupts the only salt bridge at the subunit interface of the homodimeric hemoglobin from Scapharca inaequivalvis and changes the mechanism of cooperativity.
Topics: Animals; Dimerization; Dose-Response Relationship, Drug; Escherichia coli; Heme; Hemoglobins; Hydrogen; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Mollusca; Mutagenesis, Site-Directed; Mutation; Oxygen; Protein Binding; Salts; Ultracentrifugation | 2002 |
Role of CO in attenuated vasoconstrictor reactivity of mesenteric resistance arteries after chronic hypoxia.
Topics: Animals; Blood Pressure; Carbon Monoxide; Heme; Hypoxia; Lysine; Male; Mesenteric Arteries; Nitric Oxide; Nitroarginine; Phenylephrine; Rats; Rats, Sprague-Dawley; Reference Values; Vascular Resistance; Vasoconstriction; Vasodilator Agents | 2002 |
Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure.
Topics: Amino Acid Substitution; Cyanides; Cytochrome c Group; Heme; Ligands; Lysine; Methionine; Mutation; Nuclear Magnetic Resonance, Biomolecular; Paracoccus | 2002 |
Role of the preoptic carbon monoxide pathway in endotoxin fever in rats.
Topics: Animals; Carbon Monoxide; Cyclic GMP; Deuteroporphyrins; Endotoxemia; Enzyme Inhibitors; Fever; Heme; Heme Oxygenase (Decyclizing); Injections, Intraventricular; Lipopolysaccharides; Lysine; Male; Methylene Blue; Microinjections; Preoptic Area; Rats; Rats, Wistar; Vasodilator Agents | 2002 |
An extracellular source of heme can induce a significant heme oxygenase mediated relaxation in the rat aorta.
Topics: Animals; Aorta, Thoracic; Dose-Response Relationship, Drug; Enzyme Induction; Enzyme Inhibitors; Extracellular Space; Heme; Heme Oxygenase (Decyclizing); In Vitro Techniques; Lysine; Male; Rats; Rats, Sprague-Dawley; Vasodilation | 2002 |
Carbon monoxide dilates cerebral arterioles by enhancing the coupling of Ca2+ sparks to Ca2+-activated K+ channels.
Topics: Animals; Arterioles; Calcium Channel Blockers; Calcium Signaling; Carbon Monoxide; Cells, Cultured; Cerebral Arteries; Culture Techniques; Electric Conductivity; Heme; Kinetics; Lysine; Muscle, Smooth, Vascular; Potassium Channels, Calcium-Activated; Ryanodine; Ryanodine Receptor Calcium Release Channel; Signal Transduction; Swine; Vasodilation; Vasodilator Agents | 2002 |
Central heme oxygenase-carbon monoxide pathway in the control of breathing under normoxia and hypoxia.
Topics: Animals; Carbon Monoxide; Deuteroporphyrins; Enzyme Inhibitors; Heme; Heme Oxygenase (Decyclizing); Hypoxia; Injections, Intraventricular; Lysine; Male; Rats; Rats, Wistar; Respiration; Tidal Volume; Time Factors; Ventilation | 2002 |
Endogenous carbon monoxide is an endothelial-derived vasodilator factor in the mesenteric circulation.
Topics: Animals; Aorta; Blotting, Western; Carbon Monoxide; Dose-Response Relationship, Drug; Endothelium, Vascular; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Lysine; Male; Nitric Oxide Donors; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Rats; Rats, Sprague-Dawley; Splanchnic Circulation; Vasodilation; Vasodilator Agents | 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 |
Heme oxygenase-mediated vasodilation involves vascular smooth muscle cell hyperpolarization.
Topics: Animals; Biliverdine; Calcium Signaling; Carbon Monoxide; Cell Membrane; Colforsin; Cyclic GMP; Enzyme Inhibitors; Guanylate Cyclase; Heme; Heme Oxygenase (Decyclizing); Large-Conductance Calcium-Activated Potassium Channels; Lysine; Male; Membrane Potentials; Mesenteric Arteries; Muscle, Smooth, Vascular; Potassium Channels, Calcium-Activated; Rats; Rats, Sprague-Dawley; Ryanodine; Vascular Resistance; Vasodilation | 2003 |
Proton NMR study of chemically modified horse heart ferricytochrome c confirms the presence of histidine and lysine-ligated conformers in 30% acetonitrile solution.
Topics: Acetonitriles; Animals; Cytochrome c Group; Guanidines; Heme; Histidine; Horses; Ligands; Lysine; Mitochondria, Heart; Nuclear Magnetic Resonance, Biomolecular; Organoplatinum Compounds; Protein Conformation; Protons; Solutions | 2003 |
A conformation-dependent Cotton effect in the Soret band of hemin:poly-L-lysine.
Topics: Heme; Hemin; Lysine; Molecular Conformation; Peptides | 1961 |
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 |
Hemoglobin hydrolysis and heme acquisition by Porphyromonas gingivalis.
Topics: Adhesins, Bacterial; Arginine; Cysteine Endopeptidases; Gingipain Cysteine Endopeptidases; Hemagglutinins; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Hydrolysis; Lysine; Mutation; Peptide Fragments; Porphyromonas gingivalis; Protein Binding; Virulence Factors | 2004 |
Family of cytochrome c7-type proteins from Geobacter sulfurreducens: structure of one cytochrome c7 at 1.45 A resolution.
Topics: Amino Acid Sequence; Binding Sites; Chromates; Crystallization; Crystallography, X-Ray; Cytochrome c Group; Deoxycholic Acid; Desulfuromonas; Geobacter; Glutamic Acid; Heme; Hydrophobic and Hydrophilic Interactions; Lysine; Molecular Sequence Data; Polymers; Protein Structure, Secondary; Repetitive Sequences, Amino Acid; Sequence Homology, Amino Acid | 2004 |
Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.
Topics: Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Calibration; Electron Transport Complex IV; Heme; Lysine; Methionine; Oxidation-Reduction; Paracoccus denitrificans; Phenolsulfonphthalein; Protein Subunits; Protons; Spectrophotometry | 2004 |
pH Dependence of heme iron coordination, hydrogen peroxide reactivity, and cyanide binding in cytochrome c peroxidase(H52K).
Topics: Amino Acid Substitution; Cyanides; Cytochrome-c Peroxidase; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iron; Kinetics; Lysine; Point Mutation; Protein Conformation; Protein Denaturation; Protein Structure, Secondary; Protons; Spectrum Analysis | 2004 |
Role of the conserved arginine pair in proton and electron transfer in cytochrome C oxidase.
Topics: Alanine; Arginine; Catalysis; Conserved Sequence; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Enzyme Activation; Glutamine; Heme; Kinetics; Lysine; Magnesium; Mutagenesis, Site-Directed; Photolysis; Proline; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry, Ultraviolet | 2004 |
Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base.
Topics: Binding Sites; Cystathionine beta-Synthase; Enzyme Activation; Genetic Variation; Heme; Humans; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Pyridoxal Phosphate; Recombinant Proteins; Spectrophotometry, Ultraviolet; Stereoisomerism | 2004 |
Human heme oxygenase oxidation of 5- and 15-phenylhemes.
Topics: Animals; Ascorbic Acid; Benzoic Acid; Biliverdine; Carbon Monoxide; Chromatography, High Pressure Liquid; Chromatography, Liquid; Crystallography, X-Ray; Electrons; Esters; Heme; Heme Oxygenase (Decyclizing); Horses; Humans; Ions; Lysine; Mass Spectrometry; Methionine; Models, Chemical; Models, Molecular; Myoglobin; NADPH-Ferrihemoprotein Reductase; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Spectrophotometry; Stereoisomerism; Time Factors; Ultraviolet Rays | 2004 |
The 40s Omega-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c.
Topics: Catalysis; Circular Dichroism; Cytochrome c Group; Electrochemistry; Enzyme Stability; Heme; Hydrogen-Ion Concentration; Iron; Lysine; Methionine; Oxidation-Reduction; Peptide Fragments; Protein Conformation; Protein Denaturation; Protein Folding; Spectrum Analysis, Raman | 2004 |
Endoproteolytic cleavage of human thyroperoxidase: role of the propeptide in the protein folding process.
Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Arginine; Autoantigens; Biotinylation; Brefeldin A; CHO Cells; Cricetinae; Cysteine; Cytoplasm; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Endoplasmic Reticulum; Furin; Gene Deletion; Glycosylation; Heme; Humans; Immunoprecipitation; Iodide Peroxidase; Iron-Binding Proteins; Lysine; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; Models, Genetic; Molecular Chaperones; Molecular Sequence Data; Monensin; Mutagenesis; Mutagenesis, Site-Directed; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Peptides; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Thyroid Gland; Time Factors; Transfection | 2005 |
NMR analysis of the transient complex between membrane photosystem I and soluble cytochrome c6.
Topics: Cell Membrane; Cyanobacteria; Cytochromes c6; Escherichia coli; Heme; Hydrogen; Ions; Lysine; Magnetic Resonance Spectroscopy; Models, Molecular; Nitrogen; Photosystem I Protein Complex; Protein Conformation; Software; Spectrophotometry; Static Electricity | 2005 |
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.
Topics: Binding Sites; Cell Membrane; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Hydroxyquinolines; Kinetics; Lysine; Models, Chemical; Models, Molecular; Mutation; Naphthols; Nitrate Reductase; Nitrate Reductases; Oxidoreductases; Oxygen; Pentachlorophenol; Plasmids; Protein Binding; Protons; Terpenes; Ubiquinone | 2005 |
The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus.
Topics: Amino Acid Substitution; Arginine; Binding Sites; Cytochrome b Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Lysine; Mutation; Protein Binding | 2005 |
Electrochemical and spectroscopic investigations of immobilized de novo designed heme proteins on metal electrodes.
Topics: Biophysics; Chromatography, Gel; Circular Dichroism; Electrochemistry; Electrodes; Heme; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Lysine; Mass Spectrometry; Metals; Models, Chemical; Molecular Conformation; Oxidation-Reduction; Protein Structure, Tertiary; Proteins; Spectrophotometry; Spectrum Analysis, Raman; Static Electricity; Thermodynamics; Time Factors | 2005 |
The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c-550 from Paracoccus versutus assessed by X-ray crystallography and unfolding.
Topics: Bacterial Proteins; Crystallography, X-Ray; Cytochrome c Group; Enzyme Stability; Heme; Ligands; Lysine; Methionine; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Paracoccus; Peroxidases; Protein Denaturation; Protein Structure, Tertiary; Temperature | 2005 |
Probing the stability and structure of metalloporphyrin complexes with basic peptides by mass spectrometry.
Topics: Arginine; Heme; Ions; Ligands; Lysine; Mass Spectrometry; Metalloporphyrins; Peptide Fragments; Protein Binding; Structure-Activity Relationship | 2005 |
An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase.
Topics: Animals; Arginine; Electron Transport; Electron Transport Complex IV; Enzyme Activation; Heme; Horses; Kinetics; Lysine; Mutagenesis, Site-Directed; Oxidation-Reduction; Propionates; Proton Pumps; Rhodobacter sphaeroides; Static Electricity | 2005 |
Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: a molecular dynamics comparison of the wild type and R481K mutant.
Topics: Arginine; Computer Simulation; Electron Transport Complex IV; Glutamic Acid; Heme; Hydrogen Bonding; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Propionates; Protein Structure, Secondary; Proton Pumps; Rhodobacter sphaeroides; Thermodynamics; Water | 2005 |
Monitoring circulatory heme level in hemin therapy for lowering blood pressure in rats.
Topics: Animals; Antihypertensive Agents; Blood Pressure; Dose-Response Relationship, Drug; Heme; Hemin; Hypertension; Lysine; Rats; Rats, Inbred SHR; Rats, Sprague-Dawley | 2005 |
Alteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding network.
Topics: Arginine; Binding Sites; Catalysis; Crystallography, X-Ray; Heme; Heme Oxygenase-1; Humans; Hydrogen Bonding; Kinetics; Lysine; Magnetic Resonance Spectroscopy; Mutation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation; Time Factors | 2006 |
Role of the locus coeruleus carbon monoxide pathway in endotoxin fever in rats.
Topics: Animals; Body Temperature; Carbon Monoxide; Central Nervous System; Cyclic GMP; Enzyme Inhibitors; Fever; Guanylate Cyclase; Heme; Heme Oxygenase (Decyclizing); Lipopolysaccharides; Locus Coeruleus; Lysine; Male; Rats; Rats, Wistar; Signal Transduction | 2007 |
Cofacial heme binding is linked to dimerization by a bacterial heme transport protein.
Topics: Bacterial Proteins; Biological Transport; Campylobacter jejuni; Crystallization; Dimerization; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Lysine; Models, Molecular; Mutation; Phylogeny; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Sequence Analysis, Protein; Tyrosine; Ultracentrifugation | 2006 |
Role of the peripheral heme oxygenase-carbon monoxide pathway on the nociceptive response of rats to the formalin test: evidence for a cGMP signaling pathway.
Topics: Animals; Biliverdine; Carbon Monoxide; Cyclic GMP; Deferoxamine; Deuteroporphyrins; Heme; Heme Oxygenase (Decyclizing); Iron Chelating Agents; Lysine; Male; Pain; Pain Measurement; Rats; Rats, Wistar; Signal Transduction | 2007 |
Role of prostaglandins in heme-induced fever.
Topics: Animals; Body Temperature; Brain; Dinoprostone; Dose-Response Relationship, Drug; Fever; Heme; Immunoglobulin G; Immunoglobulins; Indomethacin; Injections, Intraventricular; Lysine; Male; Rats; Rats, Sprague-Dawley | 2006 |
Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE.
Topics: Adenosine Triphosphate; Amino Acid Motifs; Aspartic Acid; ATP-Binding Cassette Transporters; Bacterial Outer Membrane Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Hydrolysis; Lysine; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Protein Subunits; Sequence Deletion | 2007 |
High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD.
Topics: Amino Acid Substitution; Benzoquinones; Cytochrome b Group; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Enzyme Stability; Escherichia coli Proteins; Heme; Hydroquinones; Lysine; Nitrate Reductase; Oxidation-Reduction; Oxidoreductases; Potentiometry; Protein Subunits; Signal Transduction; Ubiquinone; Vitamin K 2 | 2007 |
The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.
Topics: Bacterial Proteins; Crystallography, X-Ray; Cytochromes; Dimerization; Heme; Lysine; Models, Molecular; Nitrosomonas europaea; Oxidoreductases; Protein Folding; Protein Structure, Secondary | 2007 |
Alkaline conformational transition and gated electron transfer with a Lys 79 --> his variant of iso-1-cytochrome c.
Topics: Alkalies; Anaerobiosis; Cytochromes c; Electron Transport; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Magnetic Resonance Spectroscopy; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 2007 |
Role of the spinal cord heme oxygenase-carbon monoxide-cGMP pathway in the nociceptive response of rats.
Topics: Animals; Carbon Monoxide; Cyclic GMP; Deuteroporphyrins; Heme; Heme Oxygenase (Decyclizing); Lysine; Male; Methylene Blue; Pain; Rats; Rats, Sprague-Dawley; Spinal Cord | 2008 |
ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.
Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide | 2008 |
Role of locus coeruleus heme oxygenase-carbon monoxide-cGMP pathway during hypothermic response to restraint.
Topics: Animals; Behavior, Animal; Body Temperature; Carbon Monoxide; Cyclic GMP; Deuteroporphyrins; Enzyme Inhibitors; Heme; Heme Oxygenase (Decyclizing); Hypothermia; Locus Coeruleus; Lysine; Male; Microinjections; Rats; Rats, Wistar; Restraint, Physical | 2008 |
The oligomeric assembly of the novel haem-degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase.
Topics: Bacterial Proteins; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Heme; Histidine Kinase; Iron; Light; Lysine; Mutant Proteins; Mutation; Protein Binding; Protein Kinases; Protein Structure, Quaternary; Protein Structure, Secondary; Scattering, Radiation; Static Electricity; Streptomyces | 2009 |
Artemisinin dimer anticancer activity correlates with heme-catalyzed reactive oxygen species generation and endoplasmic reticulum stress induction.
Topics: Acetylcysteine; Antineoplastic Agents; Antioxidants; Apoptosis; Artemisia; Artemisinins; Biomarkers; Blotting, Western; Calcium; Cell Cycle; Dimerization; Endoplasmic Reticulum; Enzyme Inhibitors; Gene Expression Profiling; Heme; Heme Oxygenase-1; Humans; Lysine; Oligonucleotide Array Sequence Analysis; Oxidative Stress; Reactive Oxygen Species; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Thapsigargin | 2009 |
[The anti-athetotic effects of heme-L-lysinate in a rabbit model of atherosclerosis].
Topics: Animals; Atherosclerosis; Carbon Monoxide; Cholesterol, Dietary; Diet, Atherogenic; Disease Models, Animal; Heme; Heme Oxygenase-1; HSC70 Heat-Shock Proteins; Lysine; Male; Rabbits; RNA, Messenger | 2010 |
Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.
Topics: Cytochromes c; Fatty Acids; Heme; Humans; Iron; Kinetics; Lysine; Methionine; Mutation; Nitro Compounds; Oxidation-Reduction; Phenylalanine; Protein Stability; Protein Structure, Quaternary; Recombinant Proteins; Silver Compounds; Static Electricity; Sulfhydryl Compounds; Tyrosine; Water | 2012 |
Role of Met(58) in the regulation of electron/proton transfer in trihaem cytochrome PpcA from Geobacter sulfurreducens.
Topics: Bacterial Proteins; Cytochromes c; Electron Transport; Escherichia coli; Geobacter; Heme; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Solutions; Thermodynamics | 2012 |
Ubiquitination of neuronal nitric-oxide synthase in the calmodulin-binding site triggers proteasomal degradation of the protein.
Topics: Amino Acid Sequence; Animals; Binding Sites; Calmodulin; Chromatography, Liquid; HEK293 Cells; Heme; HSP70 Heat-Shock Proteins; Humans; Lysine; Mass Spectrometry; Models, Biological; Molecular Sequence Data; Mutant Proteins; Nitric Oxide Synthase Type I; Nitroarginine; Proteasome Endopeptidase Complex; Protein Binding; Proteolysis; Rats; Stereoisomerism; Substrate Specificity; Ubiquitin-Protein Ligases; Ubiquitination | 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 |
Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions.
Topics: Alanine; Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Insertional; Peptides; Protein Denaturation; Protein Stability; Protein Structure, Tertiary | 2012 |
Roles of conserved Arg(72) and Tyr(71) in the ascorbate-specific transmembrane electron transfer catalyzed by Zea mays cytochrome b561.
Topics: Arginine; Ascorbic Acid; Binding Sites; Biocatalysis; Cytochrome b Group; Electron Transport; Heme; Lysine; Mutagenesis, Site-Directed; Tyrosine; Zea mays | 2013 |
Mutation of trimethyllysine 72 to alanine enhances His79-heme-mediated dynamics of iso-1-cytochrome c.
Topics: Alanine; Amino Acid Substitution; Cytochromes c; Heme; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Stability; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 2013 |
Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand.
Topics: Chlamydomonas reinhardtii; Chloroplast Proteins; Gene Expression Regulation, Plant; Heme; Hemoglobins; Hydrogen-Ion Concentration; Lysine; Nitric Oxide; Nitrogen | 2014 |
Acute stress-induced antinociception is cGMP-dependent but heme oxygenase-independent.
Topics: Acute Pain; Animals; Carbon Monoxide; Cyclic GMP; Deuteroporphyrins; Heme; Heme Oxygenase (Decyclizing); Lysine; Male; Nociceptive Pain; Oxadiazoles; Pain Measurement; Rats, Wistar; Signal Transduction; Stress Disorders, Traumatic, Acute | 2014 |
Inactivation of myeloperoxidase by benzoic acid hydrazide.
Topics: Amino Acid Sequence; Aniline Compounds; Animals; Benzoic Acid; Carbocyanines; Catalytic Domain; Cattle; Electrons; Enzyme Inhibitors; Fluorescent Dyes; Free Radicals; Glutamic Acid; Heme; Humans; Hydrogen Peroxide; Inflammation; Lysine; Mass Spectrometry; Methionine; Molecular Conformation; Molecular Sequence Data; Neutrophils; Oxygen; Peroxidase; Spectrometry, Fluorescence | 2015 |
A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.
Topics: Animals; Apoptosis; Cardiolipins; Crystallization; Cytochromes c; Electron Spin Resonance Spectroscopy; Fungal Proteins; Heme; Horses; Hydrogen Bonding; Ions; Iron; Ligands; Lysine; Oxidation-Reduction; Oxygen; Peroxidases; Protein Binding; Protein Folding; Protein Structure, Secondary; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet | 2015 |
Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated hemoglobin with a rare histidine-lysine heme ligation.
Topics: Algal Proteins; Amino Acid Motifs; Chlamydomonas reinhardtii; Crystallography, X-Ray; Escherichia coli; Gene Expression; Heme; Histidine; Iron; Ligands; Lysine; Models, Molecular; Molecular Sequence Data; Nitrate Reductase; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Structural Homology, Protein; Truncated Hemoglobins | 2015 |
Hem12, an enzyme of heme biosynthesis pathway, is monoubiquitinated by Rsp5 ubiquitin ligase in yeast cells.
Topics: Amino Acid Motifs; Amino Acid Sequence; Down-Regulation; Endosomal Sorting Complexes Required for Transport; Gene Expression Regulation, Fungal; Glucose; Glycerol; Heme; Humans; Lysine; Molecular Conformation; Molecular Sequence Data; Mutation; Porphyria Cutanea Tarda; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Ubiquitin; Ubiquitin-Protein Ligase Complexes; Ubiquitination; Uroporphyrinogen Decarboxylase | 2015 |
Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.
Topics: Amino Acid Substitution; Binding Sites; Catalytic Domain; Electron Transport; Electron Transport Complex III; Electrons; Escherichia coli; Gene Expression; Heme; Histidine; Iron; Kinetics; Lysine; Membrane Potentials; Mutation; Quinones; Rhodobacter capsulatus; Thermodynamics | 2016 |
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 |
Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.
Topics: Amino Acid Substitution; Animals; Biocatalysis; Circular Dichroism; Cytochromes c; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Stability; Heme; Horses; Hot Temperature; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Lysine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Point Mutation; Protein Conformation; Protein Denaturation; Recombinant Proteins | 2017 |
Acetylation of lysine residues in apomyoglobin: Structural changes, amyloid fibrillation, and role of surface charge.
Topics: Acetylation; Amyloidogenic Proteins; Animals; Apoproteins; Benzothiazoles; Cell Survival; Heme; Horses; Lysine; Myoglobin; PC12 Cells; Protein Aggregates; Protein Processing, Post-Translational; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Spectrometry, Fluorescence; Static Electricity; Thiazoles | 2018 |
Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.
Topics: Amino Acid Sequence; Bacterial Proteins; Coordination Complexes; Esterification; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Lysine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Pressure; Propionates; Protein Conformation; Protein Folding; Protoporphyrins; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Static Electricity; Synechococcus; Truncated Hemoglobins | 2018 |
Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii.
Topics: Amino Acid Sequence; Chlamydomonas reinhardtii; Circular Dichroism; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Ligands; Lysine; Mutagenesis, Site-Directed; Nitric Oxide; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Conformation; Truncated Hemoglobins | 2018 |
Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1.
Topics: Amino Acid Substitution; Chlamydomonas reinhardtii; Heme; Hemoglobins; Lysine; Molecular Dynamics Simulation; Plant Proteins; Protein Conformation; Protein Stability | 2019 |
A single mutation converts Alr5027 from cyanobacteria Nostoc sp. PCC 7120 to a heme-binding protein with heme-degrading ability.
Topics: Bacterial Proteins; Binding Sites; Heme; Heme Oxygenase (Decyclizing); Histidine; Lysine; Mutation, Missense; Nostoc; Protein Binding | 2020 |
Proton-Coupled Electron Transport in Two Distinct CYBASC Paralogs of
Topics: Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Cytochrome b Group; Electron Transport; Heme; Lysine; Sequence Alignment; Tyrosine | 2020 |
Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.
Topics: Animals; Aspartic Acid; Binding Sites; Cloning, Molecular; Electrons; Escherichia coli; Ficoll; Flavin Mononucleotide; Gene Expression; Genetic Vectors; Heme; HSP90 Heat-Shock Proteins; Humans; Lysine; Molecular Docking Simulation; Mutation; NADP; Nitric Oxide Synthase Type I; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Rats; Recombinant Proteins; Static Electricity | 2020 |
Heme P460: A (Cross) Link to Nitric Oxide.
Topics: Biocatalysis; Electron Spin Resonance Spectroscopy; Heme; Hydroxylamine; Lysine; Mutagenesis; Nitric Oxide; Nitrosomonas europaea; Oxidation-Reduction; Oxidoreductases | 2020 |
Non enzymatic covalent modification by glycolysis end product converts hemoglobin into its oxidative stress potency state.
Topics: Amyloidogenic Proteins; Arginine; Coloring Agents; Congo Red; Electron Spin Resonance Spectroscopy; Glycated Hemoglobin; Glycation End Products, Advanced; Glycolysis; Glycosylation; Heme; Hemoglobins; Humans; In Vitro Techniques; Lysine; Microscopy, Electron, Scanning; Oxidation-Reduction; Oxidative Stress; Protein Aggregates; Protein Conformation; Protein Structure, Secondary; Pyruvic Acid; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2021 |
Yeast Translation Elongation Factor eIF5A Expression Is Regulated by Nutrient Availability through Different Signalling Pathways.
Topics: Aerobiosis; Carbon; Citric Acid Cycle; Down-Regulation; Eukaryotic Translation Initiation Factor 5A; Fermentation; Gene Expression Regulation, Fungal; Glucose; Heme; Iron; Iron Deficiencies; Lysine; Mechanistic Target of Rapamycin Complex 1; Metabolic Flux Analysis; Models, Biological; Nutrients; Peptide Initiation Factors; Protein Isoforms; RNA-Binding Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Signal Transduction; Up-Regulation | 2020 |
Control of distal lysine coordination in a monomeric hemoglobin: A role for heme peripheral interactions.
Topics: Chlamydomonas reinhardtii; Crystallography, X-Ray; Ferric Compounds; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Iron; Ligands; Lysine; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Oxygenases; Protein Conformation; Truncated Hemoglobins | 2021 |
Biophysical and mass spectrometry based characterization of methylglyoxal-modified myoglobin: Role of advanced glycation end products in inducing protein structural alterations.
Topics: Glycation End Products, Advanced; Heme; Hydrophobic and Hydrophilic Interactions; Lysine; Mass Spectrometry; Myoglobin; Norleucine; Protein Conformation, alpha-Helical; Protein Structure, Tertiary; Pyrroles; Pyruvaldehyde | 2021 |
Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro-l-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate.
Topics: Allylglycine; Heme; Heme Oxygenase (Decyclizing); Lysine; Oxidoreductases; Oxygen; Oxygenases; Peroxides | 2022 |