heme has been researched along with glutamic acid in 89 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 3 (3.37) | 18.7374 |
1990's | 28 (31.46) | 18.2507 |
2000's | 36 (40.45) | 29.6817 |
2010's | 20 (22.47) | 24.3611 |
2020's | 2 (2.25) | 2.80 |
Authors | Studies |
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Padmanaban, G; Surolia, N | 1 |
Boxer, SG; Gray, HB; Varadarajan, R; Zewert, TE | 1 |
Agarwal, KN; Mishra, K; Taneja, V | 1 |
Rivera, M; Walker, FA | 1 |
Choudhury, K; Marzocchi, MP; Neri, F; Poulos, TL; Smulevich, G; Willemsen, O | 1 |
Dailey, HA; Woodard, SI | 1 |
Joshi, AA; McDonald, MJ | 1 |
Doseeva, VV; Galkin, AG; Gazaryan, IG; Tishkov, VI | 1 |
Doseeva, VV; Galkin, AG; Gazarian, IG; Tishkov, VI | 1 |
Poulos, TL; Sundaramoorthy, M; Terner, J | 1 |
Kannangara, CG; von Wettstein, D; Vothknecht, UC | 1 |
Ishimori, K; Morishima, I; Tanaka, M | 2 |
Battle, A; Fukuda, H; Riley, P; Washbrook, R | 1 |
Crane, BR; Gachhui, R; Ghosh, DK; Parkinson, J; Stuehr, DJ; Wu, C | 1 |
Hashimoto, Y; Murooka, Y; Yamashita, M | 1 |
Dyer, RB; Hummer, G; Puustinen, A; Riistama, S; Wikström, M; Woodruff, WH | 1 |
Chance, MR; Friedman, JM; Goldberg, DE; Huang, S; Kloek, AP; Miller, LM; Peterson, ES; Vidugiris, G; Wang, J; Wittenberg, JB | 1 |
Brandt, U; Meunier, B; Ortwein, C; Rich, PR | 1 |
Matsuura, K; Miki, K; Nagashima, KV; Osyczka, A; Shimada, K; Sogabe, S; Yoshida, M | 1 |
Huang, ZX; Qian, W; Sun, YL; Wang, YH; Xie, Y; Zhuang, JH | 1 |
Behr, J; Grzybek, S; Hellwig, P; Ludwig, B; Mäntele, W; Michel, H | 1 |
Matsuura, K; Nagashima, KV; Osyczka, A; Shimada, K | 1 |
Bjerrum, MJ; Gleich, GJ; Højrup, P; Overgaard, MT; Oxvig, C; Sorensen, ES; Sottrup-Jensen, L; Thomsen, AR | 1 |
Kandori, H; Mogi, T; Yamazaki, Y | 1 |
Lu, Y; Wang, X | 1 |
Buse, G; Hellwig, P; Mäntele, W; Soulimane, T | 1 |
Bollen, A; Dekker, HL; Kooter, IM; Moguilevsky, N; Otto, C; Sijtsema, NM; Wever, R | 1 |
Bravo, J; Bujons, J; Ens, W; Fita, I; Hu, B; Loewen, PC; Maté, MJ; Sevinc, MS; Switala, J | 1 |
Alben, JO; Barquera, B; Brzezinski, P; Gennis, RB; Katsonouri, A; Ma, J; Puustinen, A; Thomas, JW; Tsatsos, PH; Wikström, M; Zaslavsky, D | 1 |
Pereira, MM; Teixeira, M; Verkhovskaya, ML; Verkhovsky, MI | 1 |
Azeva, TN; Gilep, AA; Lepesheva, GI; Strushkevich, NV; Usanov, SA | 1 |
Hellwig, P; Mäntele, W; Rost, B | 1 |
Malomuzh, AI; Mukhtarov, MR; Nikol'skiĭ, EE; Urazaev, AKh; Vyskocil, F | 1 |
Gennis, RB; Hellwig, P; Huang , HW; Konstantinov, AA; Moënne-Loccoz, P; Osborne, JP; Zhang, J | 1 |
Adachi, O; Devreese, B; Duine, JA; Hacisalihoglu, A; Iwabuki, H; Jongejan, JA; Kim, JK; Kuroda, S; Okajima, T; Tanizawa, K; Van Beeumen, J; Vandenberghe, I | 1 |
Bollen, A; Ferrari, RP; Ghibaudi, EM; Moguilevsky, N; Suriano, G; Watanabe, S | 1 |
Colas, C; Kuo, JM; Ortiz de Montellano, PR | 1 |
Borisov, VB; Gennis, RB; Konstantinov, AA; Liebl, U; Martin, JL; Rappaport, F; Vos, MH; Zhang, J | 1 |
Lübben, M; Ludovici, C; Prutsch, A; Vogtt, K | 1 |
Barquera, B; Gennis, RB; Gu, G; Morgan, JE; Tomson, FL; Vygodina, TV | 1 |
Baer, BR; Henne, KR; Kneller, MB; Kunze, KL; Rettie, AE; Zheng, YM | 1 |
SHIBATA, K; TOHJO, M | 1 |
Duke, NE; Londer, YY; Long, WC; Pokkuluri, PR; Schiffer, M | 1 |
Colas, C; De Montellano, PR | 1 |
Botchkareva, AE; Davydov, DR; Halpert, JR; He, YQ; Kumar, S | 1 |
Fushinobu, S; Shoun, H; Su, F; Takaya, N | 1 |
Jin, Y; Kitagawa, T; Nagai, M; Nagai, Y; Nagatomo, S | 1 |
LeBrun, LA; Limburg, J; Ortiz de Montellano, PR | 1 |
Fabian, M; Palmer, G; Parul, D | 1 |
Furtmüller, PG; Jakopitsch, C; Jantschko, W; Moguilevsky, N; Neugschwandtner, K; Obinger, C; Zederbauer, M | 1 |
Cukier, RI; Ferguson-Miller, S; Mills, DA; Seibold, SA | 1 |
Antalik, M; Fabian, M; Jancura, D; Palmer, G | 1 |
Blaney, FE; Bridges, AM; Chenery, RJ; Eggleston, DS; Jones, JJ; Lewis, CJ; Leydon, VR; Modi, S; Oxbrow, AK; Rowland, P; Smyth, MG; Tennant, MG | 1 |
Chait, BT; Fushitani, K; Gorr, TA; Kao, WY; Knapp, JE; Qin, J; Riggs, AF; Riggs, CK; Smith, SS | 1 |
Verkhovsky, MI; Wikström, M | 2 |
Olczak, T | 1 |
Collman, JP; Dinolfo, PH; Lei, J; Yan, YL | 1 |
Akimoto, S; Endou, S; Miyoshi, H; Mogi, T; Morimoto-Tadokoro, M | 1 |
Gennis, RB; Hellwig, P; Hemp, J; Hielscher, R; Miyoshi, H; Osborne, JP; Vakkasoglu, AS; Yang, K; Zhang, J | 1 |
Chubar, TA; Fechina, VA; Gazaryan, IG; Hushpulian, DM; Lagrimini, LM; Orlova, MA; Poloznikov, AA; Rozhkova, AM; Savitski, PA; Tishkov, VI | 1 |
Hummer, G; Kaila, VR; Laakkonen, L; Tuukkanen, A; Wikström, M | 1 |
Baer, BR; Kunze, KL; Rettie, AE | 1 |
Voth, GA; Xu, J | 1 |
Belevich, I; Bloch, DA; Borisov, VB; Mogi, T; Verkhovsky, MI | 1 |
Anderson, JL; Dutton, PL; Koder, RL; Moser, CC; Reddy, KS; Solomon, LA | 1 |
Berry, RE; Knipp, M; Shokhireva, TK; Walker, FA; Yang, F; Zhang, H | 1 |
Cheesman, MR; Fisher, K; Girvan, HM; Levy, CW; Leys, D; Munro, AW; Rigby, SE; Williams, P | 1 |
Davidson, VL; Goblirsch, BR; Wilmot, CM; Yukl, ET | 1 |
Ciurli, S; Daldal, F; El Khoury, Y; Francia, F; Hellwig, P; Lee, DW; Venturoli, G; Zambelli, B | 1 |
Egawa, T; Ganesan, K; Gennis, RB; Hosler, JP; Lin, MT; Rousseau, DL; Yeh, SR; Yu, MA | 1 |
Hino, T; Nagano, S; Shiro, Y; Sugimoto, H; Tosha, T | 1 |
Gennis, RB; Han, H; Hemp, J; Hosler, JP; Ouyang, H; Roh, JH | 1 |
Burton, R; Crofts, AR; Victoria, D | 1 |
Andersen, EM; Khajo, A; Koder, RL; Magliozzo, RS; Zhang, L | 1 |
Cheesman, MR; Oganesyan, VS; Richardson, DJ; Thomson, AJ; Van Wonderen, JH; Watmough, NJ | 1 |
Abu Tarboush, N; Davidson, VL; Feng, M; Shin, S; Wilmot, CM; Yukl, ET | 1 |
Chen, X; Dong, W; Fang, Y; Gong, W; Lin, Y; Liu, L; Zhao, A; Zhao, S | 1 |
Fedinec, AL; Leffler, CW; Liu, J; Parfenova, H | 1 |
Goodwin, DC; Huang, J; Panizzi, JR; Panizzi, P; Smith, F | 1 |
Altafaj, X; Alvarez, A; Bosch-Morató, M; Busquets-García, A; Fandos, C; Gomis, M; Grau, C; Guivernau, B; Ill-Raga, G; Inestrosa, N; Maldonado, R; Muñoz, FJ; Ozaita, A; Rabinowitz, MH; Ramos-Fernández, E; Rosen, MD; Tajes, M; Valls-Comamala, V; Valverde, MA; Vargas, L; Vicente, R | 1 |
Iqbal, N; Kaur, P; Sharma, S; Singh, PK; Singh, TP; Sirohi, HV; Tiwari, P | 1 |
Beare, PA; Bonazzi, M; Millar, JA; Moses, AS; Raghavan, R | 1 |
Cui, Q; Son, CY; Yethiraj, A | 1 |
Gennis, RB; Murali, R | 1 |
Abbruzzetti, S; Allegri, A; Bidon-Chanal, A; Bruno, S; Cerullo, G; Luque, FJ; Montali, C; Ogata, H; Soavi, G; Viappiani, C | 1 |
Ädelroth, P; Davydov, R; Dwaraknath, S; Hoffman, B; Kahle, M; Lu, Y; Petrik, ID; Sandoval, B | 1 |
Addis, HG; Carroll-Deaton, JA; Dang, MA; Dietz, JV; Foreman, KL; Fox, JL; Gupta, S; Hegg, EL; Khalimonchuk, O; Rivett, ED | 1 |
3 review(s) available for heme and glutamic acid
Article | Year |
---|---|
Towards the mechanism of proton pumping by the haem-copper oxidases.
Topics: Catalysis; Conserved Sequence; Glutamic Acid; Heme; Kinetics; Models, Biological; Oxidoreductases; Protons | 2006 |
The D-channel of cytochrome oxidase: an alternative view.
Topics: Biocatalysis; Copper; Cytochrome b Group; Cytochromes; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Mutation; Oxidoreductases; Proton Pumps; Protons | 2011 |
Molecular structure and function of bacterial nitric oxide reductase.
Topics: Bacterial Proteins; Cytochromes c; Glutamic Acid; Heme; Models, Molecular; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Protein Subunits; Pseudomonas aeruginosa | 2012 |
86 other study(ies) available for heme and glutamic acid
Article | Year |
---|---|
de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite.
Topics: 5-Aminolevulinate Synthetase; Aminolevulinic Acid; Animals; Glutamates; Glutamic Acid; Heme; Heptanoates; Isoleucine; Plasmodium falciparum; Porphobilinogen Synthase; Protein Biosynthesis | 1992 |
Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin.
Topics: Asparagine; Aspartic Acid; Glutamates; Glutamic Acid; Heme; Humans; Mutation; Myoglobin; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine | 1989 |
Effect of early iron deficiency in rat on the gamma-aminobutyric acid shunt in brain.
Topics: 4-Aminobutyrate Transaminase; Animals; Body Weight; Brain; Brain Chemistry; Erythrocyte Indices; Female; gamma-Aminobutyric Acid; Glutamates; Glutamic Acid; Heme; Iron Deficiencies; Isocitrate Dehydrogenase; Rats; Succinate Dehydrogenase | 1986 |
Biosynthetic preparation of isotopically labeled heme.
Topics: Aminolevulinic Acid; Animals; Carbon Isotopes; Cytochromes b5; Glutamic Acid; Heme; Isotope Labeling; Magnetic Resonance Spectroscopy; Rats | 1995 |
Effect of the His175-->Glu mutation on the heme pocket architecture of cytochrome c peroxidase.
Topics: Amino Acid Sequence; Binding Sites; Cytochrome-c Peroxidase; Glutamic Acid; Heme; Histidine; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; X-Ray Diffraction | 1995 |
Regulation of heme biosynthesis in Escherichia coli.
Topics: 5-Aminolevulinate Synthetase; Aminolevulinic Acid; Animals; Coproporphyrinogen Oxidase; Escherichia coli; Feedback; Ferrochelatase; Gene Expression Regulation, Enzymologic; Glutamic Acid; Heme; Hydroxymethylbilane Synthase; Mice; Porphyrins; Pyrroles; Rats; Recombinant Proteins; Tetrapyrroles | 1995 |
Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.
Topics: Amino Acid Sequence; Arginine; Genetic Variation; Glutamates; Glutamic Acid; Heme; Hemoglobin A; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Oxyhemoglobins; Point Mutation; Spectrophotometry; Tyrosine; Valine | 1994 |
Effect of single-point mutations Phe41-->His and Phe143-->Glu on folding and catalytic properties of recombinant horseradish peroxidase expressed in E. coli.
Topics: Base Sequence; Binding Sites; Catalysis; Escherichia coli; Glutamic Acid; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Protein Folding; Recombinant Proteins; Structure-Activity Relationship | 1994 |
[Production and catalytic properties of point mutants Phe41--->His and Phe143--->Glu of horseradish peroxidase, expressed in Escherichia coli].
Topics: Amino Acid Sequence; Base Sequence; Catalysis; Cloning, Molecular; DNA, Recombinant; Enzyme Stability; Escherichia coli; Glutamic Acid; Heme; Histidine; Horseradish Peroxidase; Molecular Sequence Data; Oxidation-Reduction; Phenylalanine; Point Mutation | 1995 |
The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
Topics: Amino Acid Sequence; Binding Sites; Catalysis; Chloride Peroxidase; Computer Simulation; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Fungal Proteins; Glutamic Acid; Glycosylation; Heme; Hemeproteins; Hydrogen Bonding; Iron; Mitosporic Fungi; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary; Structure-Activity Relationship | 1995 |
Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Aminolevulinic Acid; Base Sequence; Cytochromes; Escherichia coli; Glutamates; Glutamic Acid; Glutathione Transferase; Heme; Hemin; Hordeum; Molecular Sequence Data; Oxidation-Reduction; Recombinant Fusion Proteins; Spectrophotometry | 1996 |
The distal glutamic acid as an acid-base catalyst in the distal site of horseradish peroxidase.
Topics: Amino Acid Sequence; Binding Sites; Chloride Peroxidase; Glutamic Acid; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Oxidation-Reduction; Polymerase Chain Reaction; Recombinant Proteins; Spectrophotometry | 1996 |
Stimulation of tetrapyrrole synthesis in mammalian epithelial cells in culture by exposure to aminolaevulinic acid.
Topics: Aminolevulinic Acid; Animals; Arginine; Biological Transport; Carbon Radioisotopes; Cattle; Cell Division; Cell Line; Cycloheximide; Dactinomycin; Epithelium; gamma-Aminobutyric Acid; Glutamic Acid; Heme; Kinetics; Leucine; Mammals; Pyrroles; Radioisotope Dilution Technique; Tetrapyrroles | 1997 |
Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding.
Topics: Alanine; Amino Acid Sequence; Animals; Antioxidants; Arginine; Biopterins; Cattle; Chromatography, Gel; Glutamic Acid; Heme; Humans; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Oxygenases; Rats; Structure-Activity Relationship | 1997 |
The Propionibacterium freudenreichii hemYHBXRL gene cluster, which encodes enzymes and a regulator involved in the biosynthetic pathway from glutamate to protoheme.
Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Base Sequence; Carrier Proteins; Chromosome Mapping; DNA, Bacterial; Escherichia coli; Ferrochelatase; Genetic Complementation Test; Glutamic Acid; Heme; Intramolecular Transferases; Isomerases; Methyltransferases; Molecular Sequence Data; Open Reading Frames; Operon; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Plasmids; Porphobilinogen Synthase; Propionibacterium; Protoporphyrinogen Oxidase; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Transcription, Genetic | 1997 |
Bound water in the proton translocation mechanism of the haem-copper oxidases.
Topics: Amino Acid Sequence; Binding Sites; Cloning, Molecular; Conserved Sequence; Copper; Cytochrome b Group; Cytochromes; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Ion Channels; Ligands; Models, Chemical; Models, Molecular; Models, Statistical; Oxidation-Reduction; Protein Conformation; Protons; Water | 1997 |
A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata).
Topics: Amino Acid Substitution; Animals; Ascaris suum; Binding Sites; Bivalvia; Carbon Monoxide; Carboxyhemoglobin; Glutamic Acid; Heme; Hemoglobins; Kinetics; Oxyhemoglobins; Protein Conformation; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Thermodynamics; Tyrosine | 1997 |
Structural roles of the highly conserved glu residue in the heme distal site of peroxidases.
Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Conserved Sequence; Glutamic Acid; Heme; Horseradish Peroxidase; Hydrogen Bonding; Kinetics; Magnetic Resonance Spectroscopy; Point Mutation; Recombinant Proteins; Spectrum Analysis, Raman | 1998 |
Effects of mutation of residue I67 on redox-linked protonation processes in yeast cytochrome c oxidase.
Topics: Asparagine; Electron Transport Complex IV; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Isoleucine; Kinetics; Macromolecular Substances; Models, Molecular; Oxidation-Reduction; Point Mutation; Potentiometry; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae | 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 |
The influence of mutation at Glu44 and Glu56 of cytochrome b5 on the protein's stabilization and interaction between cytochrome c and cytochrome b5.
Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes b5; Electrochemistry; Energy Transfer; Entropy; Enzyme Stability; Glutamic Acid; Heme; Horses; Hot Temperature; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Solutions; Temperature; Urea | 1998 |
Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: separation of heme a and a3 contributions and assignment of vibrational modes.
Topics: Arginine; Aspartic Acid; Electrochemistry; Electron Transport Complex IV; Glutamic Acid; Heme; Molecular Conformation; Oxidation-Reduction; Paracoccus denitrificans; Porphyrins; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Tyrosine | 1999 |
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 |
Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo.
Topics: Amino Acid Sequence; Aspartic Acid; Chromatography, High Pressure Liquid; Eosinophil Peroxidase; Eosinophils; Esters; Glutamic Acid; Heme; Humans; Lactoperoxidase; Molecular Sequence Data; Oligopeptides; Peroxidases; Sequence Analysis | 1999 |
Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy.
Topics: Binding Sites; Copper; Cyanides; Cytochrome b Group; Cytochromes; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Mutation; Oxidation-Reduction; Protein Conformation; Riboflavin; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis | 1999 |
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Topics: Arginine; Aspartic Acid; Binding Sites; Cyanides; Cytochrome-c Peroxidase; Glutamic Acid; Glycine; Heme; Histidine; Leucine; Molecular Mimicry; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Engineering; Protons; Spectrophotometry; Valine | 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 |
Characterization of the Asp94 and Glu242 mutants in myeloperoxidase, the residues linking the heme group via ester bonds.
Topics: Aspartic Acid; Esters; Glutamic Acid; Heme; Kinetics; Mutagenesis, Site-Directed; Peroxidase; Spectrum Analysis, Raman | 1999 |
Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Base Sequence; Catalase; Crystallography, X-Ray; Cysteine; Escherichia coli; Genetic Variation; Glutamic Acid; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Recombinant Proteins; Restriction Mapping | 1999 |
Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidase.
Topics: Alanine; Conserved Sequence; Copper; Cytochrome b Group; Cytochromes; Electron Transport Complex IV; Enzyme Activation; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Membrane Proteins; Oxidation-Reduction; Proton Pumps; Quinone Reductases; Spectrophotometry, Ultraviolet; Static Electricity | 1999 |
The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump.
Topics: Amino Acid Sequence; Copper; Cytochrome c Group; Electron Transport Complex IV; Glutamic Acid; Gram-Negative Aerobic Bacteria; Heme; Liposomes; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Protein Conformation; Proteolipids; Proton Pumps; Sequence Alignment; Sequence Homology, Amino Acid; Tyrosine | 2000 |
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 |
Redox dependent conformational changes in the mixed valence form of the cytochrome c oxidase from p. The reorganization of glutamic acid 278 is coupled to the electron transfer from/to heme a and the binuclear center. denitrificans.
Topics: Electron Transport; Electron Transport Complex IV; Glutamic Acid; Heme; Oxidation-Reduction; Paracoccus denitrificans; Protein Conformation; Spectroscopy, Fourier Transform Infrared | 2001 |
[Effect of glutamate on spontaneous secretion of acetylcholine in the nerve-muscle synapse in rats].
Topics: Acetylcholine; Animals; Diaphragm; Enzyme Inhibitors; Glutamic Acid; Heme; In Vitro Techniques; Motor Endplate; Neuromuscular Junction; Nitric Oxide; Nitric Oxide Synthase; Rats | 2001 |
Site-directed mutation of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595.
Topics: Alanine; Amino Acid Sequence; Carbon Monoxide; Conserved Sequence; Cyanides; Cytochrome b Group; Cytochromes; Electrochemistry; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Oxidoreductases, N-Demethylating; Protein Binding; Protein Structure, Tertiary; Quinone Reductases; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman | 2001 |
The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond.
Topics: Amino Acid Sequence; Amino Acids; Cloning, Molecular; Cross-Linking Reagents; Cysteine; Glutamic Acid; Heme; Indolequinones; Mass Spectrometry; Models, Chemical; Models, Genetic; Molecular Sequence Data; Open Reading Frames; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Protein Binding; Protein Processing, Post-Translational; Pseudomonas putida; Quinones; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfides; Tryptophan; X-Rays | 2001 |
Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages between heme group and apo-Protein in bovine lactoperoxidase.
Topics: Amino Acid Substitution; Animals; Aspartic Acid; Base Sequence; Blotting, Western; Cattle; CHO Cells; Cricetinae; DNA Primers; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Glutamic Acid; Glycine; Heme; Lactoperoxidase; Mutation; Valine | 2001 |
Asp-225 and glu-375 in autocatalytic attachment of the prosthetic heme group of lactoperoxidase.
Topics: Animals; Aspartic Acid; Binding Sites; Catalysis; Cattle; Cell Line; Chromatography, High Pressure Liquid; Cloning, Molecular; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Gas Chromatography-Mass Spectrometry; Glutamic Acid; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Insecta; Iron; Lactoperoxidase; Models, Chemical; Models, Molecular; Mutation; Porphyrins; Protein Conformation; Protoporphyrins; Recombinant Proteins; Spectrophotometry | 2002 |
Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy.
Topics: Alanine; Amino Acid Substitution; Animals; Binding Sites; Carbon Monoxide; Cell Membrane; Escherichia coli; Glutamic Acid; Heme; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Oxidoreductases; Oxygen; Photolysis; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet | 2002 |
Electron transfer at the low-spin heme b of cytochrome bo(3) induces an environmental change of the catalytic enhancer glutamic acid-286.
Topics: Catalytic Domain; Copper; Cytochrome b Group; Cytochromes; Electron Transport; Escherichia coli Proteins; Glutamic Acid; Heme; Models, Chemical; Models, Molecular; Oxidation-Reduction; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship | 2002 |
Substitutions for glutamate 101 in subunit II of cytochrome c oxidase from Rhodobacter sphaeroides result in blocking the proton-conducting K-channel.
Topics: Amino Acid Substitution; Conserved Sequence; Electron Transport; Electron Transport Complex IV; Glutamic Acid; Heme; Hydrogen Peroxide; Mutagenesis, Site-Directed; Oxidants; Oxidation-Reduction; Protein Structure, Secondary; Protein Subunits; Proton Pump Inhibitors; Proton Pumps; Protons; Rhodobacter sphaeroides; Spectrophotometry, Ultraviolet | 2003 |
Covalent heme binding to CYP4B1 via Glu310 and a carbocation porphyrin intermediate.
Topics: Aryl Hydrocarbon Hydroxylases; Dimerization; Glutamic Acid; Heme; Lauric Acids; Mutation; Oxygen; Porphyrins | 2003 |
ABSORPTION SPECTRA OF HEMATIN COMPLEXES WITH POLYHISTIDINE AND COPOLY-(HISTIDINE, GLUTAMIC ACID).
Topics: Animals; Cytochromes; Glutamates; Glutamic Acid; Heme; Hemin; Histidine; Horses; Methemoglobin; Peptides; Research; Spectrophotometry | 1963 |
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 |
Horseradish peroxidase mutants that autocatalytically modify their prosthetic heme group: insights into mammalian peroxidase heme-protein covalent bonds.
Topics: Animals; Carboxylic Acids; Catalysis; Cell Line; Chromatography, High Pressure Liquid; Cloning, Molecular; DNA; Electrophoresis, Polyacrylamide Gel; Genetic Variation; Glutamic Acid; Glycine; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Insecta; Kinetics; Leucine; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Peroxidase; Phenylalanine; Porphyrins; Protein Structure, Secondary; Serine; Spectrophotometry; Time Factors; Ultraviolet Rays | 2004 |
An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF.
Topics: Allosteric Site; Amino Acid Substitution; Bacterial Proteins; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Fluorescence Resonance Energy Transfer; Glutamic Acid; Heme; Mixed Function Oxygenases; Osmolar Concentration; Protein Conformation; Protein Structure, Secondary; Pyrenes; Static Electricity | 2004 |
Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome p450nor.
Topics: Amino Acid Substitution; Arginine; Aspartic Acid; Cytochrome P-450 Enzyme System; Fusarium; Glutamic Acid; Heme; Molecular Structure; NAD; Oxidoreductases; Point Mutation | 2004 |
Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy.
Topics: Carbon; Glutamic Acid; Heme; Hemoglobin M; Hemoglobins; Hemoglobins, Abnormal; Histidine; Ions; Models, Chemical; Mutation; Oxygen; Spectrum Analysis, Raman; Tyrosine | 2004 |
The P450cam G248E mutant covalently binds its prosthetic heme group.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Camphor; Camphor 5-Monooxygenase; Catalysis; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System; Glutamic Acid; Glycine; Heme; Humans; Hydroxylation; Isoenzymes; Models, Chemical; Models, Molecular; Molecular Sequence Data; Protein Binding; Rats | 2005 |
Proton interactions with hemes a and a3 in bovine heart cytochrome c oxidase.
Topics: Animals; Catalysis; Cattle; Electron Transport Complex IV; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Kinetics; Mitochondria, Heart; Oxidation-Reduction; Potassium Channels; Protein Subunits; Protons; Spectrophotometry | 2005 |
Role of the covalent glutamic acid 242-heme linkage in the formation and reactivity of redox intermediates of human myeloperoxidase.
Topics: Animals; Aspartic Acid; Binding Sites; Bromides; Chlorides; CHO Cells; Circular Dichroism; Cricetinae; Cyanides; Enzyme Stability; Eosinophil Peroxidase; Ferric Compounds; Glutamic Acid; Glutamine; Heme; Humans; Methionine; Oxidation-Reduction; Peroxidase; Recombinant Proteins | 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 |
A role for the protein in internal electron transfer to the catalytic center of cytochrome c oxidase.
Topics: Animals; Catalytic Domain; Cattle; Detergents; Electron Transport; Electron Transport Complex IV; Electrons; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Ion Transport; Kinetics; Oxidation-Reduction; Protons | 2005 |
Crystal structure of human cytochrome P450 2D6.
Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Cytochrome P-450 CYP2D6; Glutamic Acid; Heme; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Software; Subcellular Fractions; Substrate Specificity | 2006 |
Linker chains of the gigantic hemoglobin of the earthworm Lumbricus terrestris: primary structures of linkers L2, L3, and L4 and analysis of the connectivity of the disulfide bonds in linker L1.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Binding Sites; Calcium; Chromatography, High Pressure Liquid; Cysteine; Disulfides; Dithiothreitol; DNA, Complementary; Glutamic Acid; Heme; Hemoglobins; Histidine; Humans; Ligands; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Oligochaeta; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Receptors, LDL; RNA, Messenger; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Superoxide Dismutase | 2006 |
Analysis of conserved glutamate residues in Porphyromonas gingivalis outer membrane receptor HmuR: toward a further understanding of heme uptake.
Topics: Albumins; Amino Acid Sequence; Amino Acid Substitution; Bacterial Outer Membrane Proteins; Culture Media; Glutamic Acid; Heme; Hemoglobins; Humans; Molecular Sequence Data; Periodontitis; Point Mutation; Porphyromonas gingivalis; Protein Binding; Receptors, Cell Surface; Sequence Alignment; Virulence | 2006 |
Active-site models of bacterial nitric oxide reductase featuring tris-histidyl and glutamic acid mimics: influence of a carboxylate ligand on Fe(B) binding and the heme Fe/Fe(B) redox potential.
Topics: Bacterial Proteins; Binding Sites; Biomimetic Materials; Carboxylic Acids; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Imidazoles; Iron; Ligands; Metalloporphyrins; Models, Molecular; Molecular Structure; Oxidation-Reduction; Oxidoreductases | 2006 |
Glutamates 99 and 107 in transmembrane helix III of subunit I of cytochrome bd are critical for binding of the heme b595-d binuclear center and enzyme activity.
Topics: Aerobiosis; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Conserved Sequence; Cytochrome b Group; Cytochromes; Electron Transport Chain Complex Proteins; Enzyme Activation; Escherichia coli Proteins; Glutamic Acid; Heme; Leucine; Membrane Proteins; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxygen; Oxygen Consumption; Protein Structure, Secondary; Protein Subunits; Ubiquinone | 2006 |
Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center.
Topics: Amino Acid Sequence; Cytochrome b Group; Cytochromes; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Spectroscopy, Fourier Transform Infrared | 2007 |
Glutamic acid-141: a heme 'bodyguard' in anionic tobacco peroxidase.
Topics: Amino Acid Sequence; Amino Acid Substitution; Benzothiazoles; Dianisidine; Gamma Rays; Glutamic Acid; Guaiacol; Heme; Nicotiana; Peroxidases; Protein Folding; Recombinant Proteins; Substrate Specificity; Sulfonic Acids | 2007 |
Dynamics of the glutamic acid 242 side chain in cytochrome c oxidase.
Topics: Animals; Cattle; Electron Transport Complex IV; Glutamic Acid; Heme; Models, Biological; Models, Molecular; Molecular Conformation; Myocardium; Oxygen; Proton Pumps; Protons; Time Factors; Water | 2007 |
Mechanism of formation of the ester linkage between heme and Glu310 of CYP4B1: 18O protein labeling studies.
Topics: Amino Acid Sequence; Aryl Hydrocarbon Hydroxylases; Aspartic Acid; Binding Sites; Esters; Glutamic Acid; Heme; Kinetics; Mass Spectrometry; Peptide Fragments; Polymerase Chain Reaction; Recombinant Proteins; Trypsin | 2007 |
Redox-coupled proton pumping in cytochrome c oxidase: further insights from computer simulation.
Topics: Computer Simulation; Electron Transport Complex IV; Glutamic Acid; Heme; Membrane Proteins; Models, Molecular; Oxidation-Reduction; Proton Pumps; Saccharomyces cerevisiae Proteins | 2008 |
Glutamate 107 in subunit I of cytochrome bd from Escherichia coli is part of a transmembrane intraprotein pathway conducting protons from the cytoplasm to the heme b595/heme d active site.
Topics: Binding Sites; Carbon Monoxide; Cytochrome b Group; Cytochromes; Cytoplasm; Electrochemistry; Electron Transport Chain Complex Proteins; Escherichia coli Proteins; Glutamic Acid; Heme; Leucine; Mutagenesis, Site-Directed; Mutation; Oxidoreductases; Photolysis; Protein Binding; Protons | 2008 |
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 |
1H and 13C NMR spectroscopic studies of the ferriheme resonances of three low-spin complexes of wild-type nitrophorin 2 and nitrophorin 2(V24E) as a function of pH.
Topics: Animals; Cyanides; Gene Expression; Glutamic Acid; Heme; Hemeproteins; Hemin; Histamine; Hydrogen Bonding; Hydrogen-Ion Concentration; Imidazoles; Insect Proteins; Ligands; Models, Molecular; Mutant Proteins; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Recombinant Proteins; Rhodnius; Salivary Proteins and Peptides | 2009 |
Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.
Topics: Arachidonic Acid; Bacterial Proteins; Crystallography; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Esters; Glutamic Acid; Heme; Kinetics; Lauric Acids; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Potentiometry; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Substrate Specificity | 2010 |
Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Biocatalysis; Carbon Monoxide; Crystallography, X-Ray; Cytochrome-c Peroxidase; Ferrous Compounds; Glutamic Acid; Heme; Hemeproteins; Indolequinones; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nitric Oxide; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity; Tryptophan | 2011 |
Zinc inhibition of bacterial cytochrome bc(1) reveals the role of cytochrome b E295 in proton release at the Q(o) site.
Topics: Calorimetry; Catalytic Domain; Electron Transport Complex III; Enzyme Inhibitors; Glutamic Acid; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protons; Rhodobacter capsulatus; Spectroscopy, Fourier Transform Infrared; Zinc | 2011 |
Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.
Topics: Catalytic Domain; Copper; Cytochrome b Group; Cytochromes; Electron Transport; Electron Transport Complex IV; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Models, Molecular; Mutation; Oxidoreductases; Protein Binding; Protein Conformation; Protons; Rhodobacter sphaeroides; Species Specificity; Spectrum Analysis, Raman | 2011 |
Functional importance of a pair of conserved glutamic acid residues and of Ca(2+) binding in the cbb(3)-type oxygen reductases from Rhodobacter sphaeroides and Vibrio cholerae.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Calcium; Electron Transport Complex IV; Glutamic Acid; Heme; Mutation, Missense; Oxidation-Reduction; Protein Binding; Protein Subunits; Rhodobacter sphaeroides; Vibrio cholerae | 2012 |
Role of the -PEWY-glutamate in catalysis at the Q(o)-site of the Cyt bc(1) complex.
Topics: Antimycin A; Biocatalysis; Electron Transport Complex III; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Hydroquinones; Oxidation-Reduction; Protons | 2013 |
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 |
Unexpected weak magnetic exchange coupling between haem and non-haem iron in the catalytic site of nitric oxide reductase (NorBC) from Paracoccus denitrificans1.
Topics: Bacterial Proteins; Catalytic Domain; Circular Dichroism; Electron Spin Resonance Spectroscopy; Glutamic Acid; Heme; Iron; Kinetics; Magnetic Phenomena; Oxidation-Reduction; Oxidoreductases; Paracoccus denitrificans; Thermodynamics | 2013 |
Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.
Topics: Crystallography, X-Ray; Ferric Compounds; Ferrous Compounds; Glutamic Acid; Heme; Hemeproteins; Hydrogen Peroxide; Indolequinones; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan | 2013 |
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Binding Sites; Crystallography, X-Ray; Glutamates; Glutamic Acid; Heme; Models, Molecular; Molecular Sequence Data; Multiprotein Complexes; NADP; Protein Interaction Domains and Motifs; Recombinant Proteins; RNA-Binding Proteins; Sequence Homology, Amino Acid; Static Electricity | 2014 |
Enteral supplements of a carbon monoxide donor CORM-A1 protect against cerebrovascular dysfunction caused by neonatal seizures.
Topics: Adenosine Diphosphate; Animals; Arterioles; Boranes; Bradykinin; Carbon Monoxide; Carbonates; Cerebrovascular Circulation; Cerebrovascular Disorders; Dietary Supplements; Excitatory Amino Acid Agonists; Female; Glutamic Acid; Heme; Male; Quisqualic Acid; Seizures; Swine; Time Factors; Vasodilator Agents | 2015 |
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 |
Glutamatergic stimulation induces GluN2B translation by the nitric oxide-Heme-Regulated eIF2α kinase in cortical neurons.
Topics: Animals; Cells, Cultured; Cerebellar Cortex; Disks Large Homolog 4 Protein; Eukaryotic Initiation Factor-2; Excitatory Amino Acid Agents; Glutamic Acid; Heme; Humans; Memory; Mice; Mice, Inbred Strains; Neurons; Nitric Oxide; Phosphorylation; Protein Biosynthesis; Receptors, N-Methyl-D-Aspartate; RNA, Small Interfering | 2016 |
Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution.
Topics: Animals; Aspartic Acid; Binding Sites; Cattle; Crystallography, X-Ray; Glutamic Acid; Heme; Lactoperoxidase; Mammals; Models, Molecular; Peroxidase; Protein Conformation | 2017 |
Horizontally Acquired Biosynthesis Genes Boost
Topics: Biotin; Coxiella burnetii; Fatty Acids; Gene Transfer, Horizontal; Genes, Bacterial; Glutamic Acid; Heme; Lipopolysaccharides; Metabolic Networks and Pathways; RNA, Ribosomal, 16S; Viral Proteins | 2017 |
Cavity hydration dynamics in cytochrome
Topics: Electron Transport Complex IV; Glutamic Acid; Heme; Models, Molecular; Molecular Dynamics Simulation; Oxidation-Reduction; Propionates; Protons; Rhodobacter sphaeroides; Static Electricity; Thermodynamics; Water | 2017 |
Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli.
Topics: Cell Respiration; Cytochrome b Group; Cytochromes; Electron Transport; Electron Transport Chain Complex Proteins; Electrons; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxidoreductases; Oxygen; Protons | 2018 |
Electrostatic Tuning of the Ligand Binding Mechanism by Glu27 in Nitrophorin 7.
Topics: Animals; Crystallography, X-Ray; Glutamic Acid; Heme; Hemeproteins; Insect Proteins; Ligands; Models, Molecular; Molecular Dynamics Simulation; Mutation; Protein Conformation; Rhodnius; Salivary Proteins and Peptides; Static Electricity | 2018 |
An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network.
Topics: Copper; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Metabolic Engineering; Models, Biological; Oxidoreductases | 2021 |
Evidence that the catalytic mechanism of heme a synthase involves the formation of a carbocation stabilized by a conserved glutamate.
Topics: Ferrochelatase; Glutamic Acid; Heme; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2023 |