Compounds > heme
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heme and glutamic acid

heme has been researched along with glutamic acid in 89 studies

Research

Studies (89)

TimeframeStudies, this research(%)All Research%
pre-19903 (3.37)18.7374
1990's28 (31.46)18.2507
2000's36 (40.45)29.6817
2010's20 (22.47)24.3611
2020's2 (2.25)2.80

Authors

AuthorsStudies
Padmanaban, G; Surolia, N1
Boxer, SG; Gray, HB; Varadarajan, R; Zewert, TE1
Agarwal, KN; Mishra, K; Taneja, V1
Rivera, M; Walker, FA1
Choudhury, K; Marzocchi, MP; Neri, F; Poulos, TL; Smulevich, G; Willemsen, O1
Dailey, HA; Woodard, SI1
Joshi, AA; McDonald, MJ1
Doseeva, VV; Galkin, AG; Gazaryan, IG; Tishkov, VI1
Doseeva, VV; Galkin, AG; Gazarian, IG; Tishkov, VI1
Poulos, TL; Sundaramoorthy, M; Terner, J1
Kannangara, CG; von Wettstein, D; Vothknecht, UC1
Ishimori, K; Morishima, I; Tanaka, M2
Battle, A; Fukuda, H; Riley, P; Washbrook, R1
Crane, BR; Gachhui, R; Ghosh, DK; Parkinson, J; Stuehr, DJ; Wu, C1
Hashimoto, Y; Murooka, Y; Yamashita, M1
Dyer, RB; Hummer, G; Puustinen, A; Riistama, S; Wikström, M; Woodruff, WH1
Chance, MR; Friedman, JM; Goldberg, DE; Huang, S; Kloek, AP; Miller, LM; Peterson, ES; Vidugiris, G; Wang, J; Wittenberg, JB1
Brandt, U; Meunier, B; Ortwein, C; Rich, PR1
Matsuura, K; Miki, K; Nagashima, KV; Osyczka, A; Shimada, K; Sogabe, S; Yoshida, M1
Huang, ZX; Qian, W; Sun, YL; Wang, YH; Xie, Y; Zhuang, JH1
Behr, J; Grzybek, S; Hellwig, P; Ludwig, B; Mäntele, W; Michel, H1
Matsuura, K; Nagashima, KV; Osyczka, A; Shimada, K1
Bjerrum, MJ; Gleich, GJ; Højrup, P; Overgaard, MT; Oxvig, C; Sorensen, ES; Sottrup-Jensen, L; Thomsen, AR1
Kandori, H; Mogi, T; Yamazaki, Y1
Lu, Y; Wang, X1
Buse, G; Hellwig, P; Mäntele, W; Soulimane, T1
Bollen, A; Dekker, HL; Kooter, IM; Moguilevsky, N; Otto, C; Sijtsema, NM; Wever, R1
Bravo, J; Bujons, J; Ens, W; Fita, I; Hu, B; Loewen, PC; Maté, MJ; Sevinc, MS; Switala, J1
Alben, JO; Barquera, B; Brzezinski, P; Gennis, RB; Katsonouri, A; Ma, J; Puustinen, A; Thomas, JW; Tsatsos, PH; Wikström, M; Zaslavsky, D1
Pereira, MM; Teixeira, M; Verkhovskaya, ML; Verkhovsky, MI1
Azeva, TN; Gilep, AA; Lepesheva, GI; Strushkevich, NV; Usanov, SA1
Hellwig, P; Mäntele, W; Rost, B1
Malomuzh, AI; Mukhtarov, MR; Nikol'skiĭ, EE; Urazaev, AKh; Vyskocil, F1
Gennis, RB; Hellwig, P; Huang , HW; Konstantinov, AA; Moënne-Loccoz, P; Osborne, JP; Zhang, J1
Adachi, O; Devreese, B; Duine, JA; Hacisalihoglu, A; Iwabuki, H; Jongejan, JA; Kim, JK; Kuroda, S; Okajima, T; Tanizawa, K; Van Beeumen, J; Vandenberghe, I1
Bollen, A; Ferrari, RP; Ghibaudi, EM; Moguilevsky, N; Suriano, G; Watanabe, S1
Colas, C; Kuo, JM; Ortiz de Montellano, PR1
Borisov, VB; Gennis, RB; Konstantinov, AA; Liebl, U; Martin, JL; Rappaport, F; Vos, MH; Zhang, J1
Lübben, M; Ludovici, C; Prutsch, A; Vogtt, K1
Barquera, B; Gennis, RB; Gu, G; Morgan, JE; Tomson, FL; Vygodina, TV1
Baer, BR; Henne, KR; Kneller, MB; Kunze, KL; Rettie, AE; Zheng, YM1
SHIBATA, K; TOHJO, M1
Duke, NE; Londer, YY; Long, WC; Pokkuluri, PR; Schiffer, M1
Colas, C; De Montellano, PR1
Botchkareva, AE; Davydov, DR; Halpert, JR; He, YQ; Kumar, S1
Fushinobu, S; Shoun, H; Su, F; Takaya, N1
Jin, Y; Kitagawa, T; Nagai, M; Nagai, Y; Nagatomo, S1
LeBrun, LA; Limburg, J; Ortiz de Montellano, PR1
Fabian, M; Palmer, G; Parul, D1
Furtmüller, PG; Jakopitsch, C; Jantschko, W; Moguilevsky, N; Neugschwandtner, K; Obinger, C; Zederbauer, M1
Cukier, RI; Ferguson-Miller, S; Mills, DA; Seibold, SA1
Antalik, M; Fabian, M; Jancura, D; Palmer, G1
Blaney, FE; Bridges, AM; Chenery, RJ; Eggleston, DS; Jones, JJ; Lewis, CJ; Leydon, VR; Modi, S; Oxbrow, AK; Rowland, P; Smyth, MG; Tennant, MG1
Chait, BT; Fushitani, K; Gorr, TA; Kao, WY; Knapp, JE; Qin, J; Riggs, AF; Riggs, CK; Smith, SS1
Verkhovsky, MI; Wikström, M2
Olczak, T1
Collman, JP; Dinolfo, PH; Lei, J; Yan, YL1
Akimoto, S; Endou, S; Miyoshi, H; Mogi, T; Morimoto-Tadokoro, M1
Gennis, RB; Hellwig, P; Hemp, J; Hielscher, R; Miyoshi, H; Osborne, JP; Vakkasoglu, AS; Yang, K; Zhang, J1
Chubar, TA; Fechina, VA; Gazaryan, IG; Hushpulian, DM; Lagrimini, LM; Orlova, MA; Poloznikov, AA; Rozhkova, AM; Savitski, PA; Tishkov, VI1
Hummer, G; Kaila, VR; Laakkonen, L; Tuukkanen, A; Wikström, M1
Baer, BR; Kunze, KL; Rettie, AE1
Voth, GA; Xu, J1
Belevich, I; Bloch, DA; Borisov, VB; Mogi, T; Verkhovsky, MI1
Anderson, JL; Dutton, PL; Koder, RL; Moser, CC; Reddy, KS; Solomon, LA1
Berry, RE; Knipp, M; Shokhireva, TK; Walker, FA; Yang, F; Zhang, H1
Cheesman, MR; Fisher, K; Girvan, HM; Levy, CW; Leys, D; Munro, AW; Rigby, SE; Williams, P1
Davidson, VL; Goblirsch, BR; Wilmot, CM; Yukl, ET1
Ciurli, S; Daldal, F; El Khoury, Y; Francia, F; Hellwig, P; Lee, DW; Venturoli, G; Zambelli, B1
Egawa, T; Ganesan, K; Gennis, RB; Hosler, JP; Lin, MT; Rousseau, DL; Yeh, SR; Yu, MA1
Hino, T; Nagano, S; Shiro, Y; Sugimoto, H; Tosha, T1
Gennis, RB; Han, H; Hemp, J; Hosler, JP; Ouyang, H; Roh, JH1
Burton, R; Crofts, AR; Victoria, D1
Andersen, EM; Khajo, A; Koder, RL; Magliozzo, RS; Zhang, L1
Cheesman, MR; Oganesyan, VS; Richardson, DJ; Thomson, AJ; Van Wonderen, JH; Watmough, NJ1
Abu Tarboush, N; Davidson, VL; Feng, M; Shin, S; Wilmot, CM; Yukl, ET1
Chen, X; Dong, W; Fang, Y; Gong, W; Lin, Y; Liu, L; Zhao, A; Zhao, S1
Fedinec, AL; Leffler, CW; Liu, J; Parfenova, H1
Goodwin, DC; Huang, J; Panizzi, JR; Panizzi, P; Smith, F1
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, R1
Iqbal, N; Kaur, P; Sharma, S; Singh, PK; Singh, TP; Sirohi, HV; Tiwari, P1
Beare, PA; Bonazzi, M; Millar, JA; Moses, AS; Raghavan, R1
Cui, Q; Son, CY; Yethiraj, A1
Gennis, RB; Murali, R1
Abbruzzetti, S; Allegri, A; Bidon-Chanal, A; Bruno, S; Cerullo, G; Luque, FJ; Montali, C; Ogata, H; Soavi, G; Viappiani, C1
Ädelroth, P; Davydov, R; Dwaraknath, S; Hoffman, B; Kahle, M; Lu, Y; Petrik, ID; Sandoval, B1
Addis, HG; Carroll-Deaton, JA; Dang, MA; Dietz, JV; Foreman, KL; Fox, JL; Gupta, S; Hegg, EL; Khalimonchuk, O; Rivett, ED1

Reviews

3 review(s) available for heme and glutamic acid

ArticleYear
Towards the mechanism of proton pumping by the haem-copper oxidases.
    Biochimica et biophysica acta, 2006, Volume: 1757, Issue:8

    Topics: Catalysis; Conserved Sequence; Glutamic Acid; Heme; Kinetics; Models, Biological; Oxidoreductases; Protons

2006
The D-channel of cytochrome oxidase: an alternative view.
    Biochimica et biophysica acta, 2011, Volume: 1807, Issue:10

    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.
    Biochimica et biophysica acta, 2012, Volume: 1817, Issue:4

    Topics: Bacterial Proteins; Cytochromes c; Glutamic Acid; Heme; Models, Molecular; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Protein Subunits; Pseudomonas aeruginosa

2012

Other Studies

86 other study(ies) available for heme and glutamic acid

ArticleYear
de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite.
    Biochemical and biophysical research communications, 1992, Sep-16, Volume: 187, Issue:2

    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.
    Science (New York, N.Y.), 1989, Jan-06, Volume: 243, Issue:4887

    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.
    Journal of neurochemistry, 1986, Volume: 46, Issue:6

    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.
    Analytical biochemistry, 1995, Sep-20, Volume: 230, Issue:2

    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.
    Biochemistry, 1995, Oct-17, Volume: 34, Issue:41

    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.
    Archives of biochemistry and biophysics, 1995, Jan-10, Volume: 316, Issue:1

    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.
    The Journal of biological chemistry, 1994, Mar-18, Volume: 269, Issue:11

    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.
    FEBS letters, 1994, Nov-14, Volume: 354, Issue:3

    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].
    Biokhimiia (Moscow, Russia), 1995, Volume: 60, Issue:10

    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.
    Structure (London, England : 1993), 1995, Dec-15, Volume: 3, Issue:12

    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.
    Proceedings of the National Academy of Sciences of the United States of America, 1996, Aug-20, Volume: 93, Issue:17

    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.
    Biochemical and biophysical research communications, 1996, Oct-14, Volume: 227, Issue:2

    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.
    British journal of cancer, 1997, Volume: 75, Issue:3

    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.
    Biochemistry, 1997, Apr-29, Volume: 36, Issue:17

    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.
    Applied microbiology and biotechnology, 1997, Volume: 47, Issue:4

    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.
    FEBS letters, 1997, Sep-08, Volume: 414, Issue:2

    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).
    Biochemistry, 1997, Oct-21, Volume: 36, Issue:42

    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.
    Biochemistry, 1998, Feb-24, Volume: 37, Issue:8

    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.
    The Biochemical journal, 1998, Mar-15, Volume: 330 ( Pt 3)

    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.
    Biochemistry, 1998, Aug-25, Volume: 37, Issue:34

    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.
    Biochemistry, 1998, Oct-06, Volume: 37, Issue:40

    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.
    Biochemistry, 1999, Feb-09, Volume: 38, Issue:6

    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.
    Biochemistry, 1999, Mar-09, Volume: 38, Issue:10

    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.
    The Journal of biological chemistry, 1999, Jun-11, Volume: 274, Issue:24

    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.
    Journal of biochemistry, 1999, Volume: 126, Issue:1

    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.
    Biochemistry, 1999, Jul-13, Volume: 38, Issue:28

    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.
    Biochemistry, 1999, Jul-27, Volume: 38, Issue:30

    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.
    European journal of biochemistry, 1999, Volume: 264, Issue:1

    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.
    The Journal of biological chemistry, 1999, Sep-24, Volume: 274, Issue:39

    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.
    Biochemistry, 1999, Nov-16, Volume: 38, Issue:46

    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.
    Biochemistry, 2000, May-30, Volume: 39, Issue:21

    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.
    Biochemistry. Biokhimiia, 2000, Volume: 65, Issue:12

    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.
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2001, Volume: 57A, Issue:5

    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].
    Rossiiskii fiziologicheskii zhurnal imeni I.M. Sechenova, 2001, Volume: 87, Issue:4

    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.
    Biochemistry, 2001, Jul-24, Volume: 40, Issue:29

    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.
    The Journal of biological chemistry, 2001, Nov-16, Volume: 276, Issue:46

    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.
    Bioorganic & medicinal chemistry letters, 2001, Nov-05, Volume: 11, Issue:21

    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.
    The Journal of biological chemistry, 2002, Mar-01, Volume: 277, Issue:9

    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.
    Biochemistry, 2002, Feb-05, Volume: 41, Issue:5

    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.
    Biochimica et biophysica acta, 2002, Apr-22, Volume: 1554, Issue:1-2

    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.
    Biochemistry, 2003, Feb-18, Volume: 42, Issue:6

    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.
    Biochemistry, 2003, Apr-22, Volume: 42, Issue:15

    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).
    Archives of biochemistry and biophysics, 1963, Volume: 103

    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.
    Biochemistry, 2004, Feb-03, Volume: 43, Issue:4

    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.
    The Journal of biological chemistry, 2004, Jun-04, Volume: 279, Issue:23

    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.
    Biochemistry, 2004, Jun-01, Volume: 43, Issue:21

    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.
    Bioscience, biotechnology, and biochemistry, 2004, Volume: 68, Issue:5

    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.
    Biochemistry, 2004, Jul-06, Volume: 43, Issue:26

    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.
    Biochemistry, 2005, Mar-15, Volume: 44, Issue:10

    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.
    Biochemistry, 2005, Mar-22, Volume: 44, Issue:11

    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.
    Biochemistry, 2005, May-03, Volume: 44, Issue:17

    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.
    Biochemistry, 2005, Aug-09, Volume: 44, Issue:31

    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.
    Biochemistry, 2005, Nov-15, Volume: 44, Issue:45

    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.
    The Journal of biological chemistry, 2006, Mar-17, Volume: 281, Issue:11

    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.
    Proteins, 2006, Apr-01, Volume: 63, Issue:1

    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.
    Archives of microbiology, 2006, Volume: 186, Issue:5

    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.
    Inorganic chemistry, 2006, Sep-18, Volume: 45, Issue:19

    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.
    Biochemistry, 2006, Dec-26, Volume: 45, Issue:51

    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.
    Biochemistry, 2007, Mar-20, Volume: 46, Issue:11

    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.
    Biological chemistry, 2007, Volume: 388, Issue:4

    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.
    Biochimica et biophysica acta, 2007, Volume: 1767, Issue:9

    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.
    Biochemistry, 2007, Oct-16, Volume: 46, Issue:41

    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.
    Biochimica et biophysica acta, 2008, Volume: 1777, Issue:2

    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.
    Biochemistry, 2008, Jul-29, Volume: 47, Issue:30

    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.
    Nature, 2009, Mar-19, Volume: 458, Issue:7236

    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.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009, Volume: 14, Issue:7

    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.
    The Biochemical journal, 2010, Apr-14, Volume: 427, Issue:3

    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.
    Biochemistry, 2011, Apr-12, Volume: 50, Issue:14

    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.
    Biochemistry, 2011, May-24, Volume: 50, Issue:20

    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.
    Biochimica et biophysica acta, 2011, Volume: 1807, Issue:10

    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.
    Biochemistry, 2012, Sep-18, Volume: 51, Issue:37

    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.
    Biochimica et biophysica acta, 2013, Volume: 1827, Issue:3

    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.
    Biochemistry, 2013, Jan-22, Volume: 52, Issue:3

    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.
    The Biochemical journal, 2013, May-01, Volume: 451, Issue:3

    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.
    Biochemistry, 2013, Sep-17, Volume: 52, Issue:37

    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.
    Proceedings of the National Academy of Sciences of the United States of America, 2014, May-06, Volume: 111, Issue:18

    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.
    Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism, 2015, Volume: 35, Issue:2

    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.
    Archives of biochemistry and biophysics, 2015, Mar-15, Volume: 570

    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.
    Oncotarget, 2016, 09-13, Volume: 7, Issue:37

    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.
    Biochimica et biophysica acta. Proteins and proteomics, 2017, Volume: 1865, Issue:3

    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
    Frontiers in cellular and infection microbiology, 2017, Volume: 7

    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
    Proceedings of the National Academy of Sciences of the United States of America, 2017, 10-17, Volume: 114, Issue:42

    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.
    Biochimica et biophysica acta. Bioenergetics, 2018, Volume: 1859, Issue:8

    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.
    Scientific reports, 2018, Jul-18, Volume: 8, Issue:1

    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.
    Biochemistry, 2021, 02-02, Volume: 60, Issue:4

    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.
    Archives of biochemistry and biophysics, 2023, Volume: 744

    Topics: Ferrochelatase; Glutamic Acid; Heme; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

2023