Compounds > heme
Page last updated: 2024-08-23

heme and flavin mononucleotide

heme has been researched along with flavin mononucleotide in 120 studies

Research

Studies (120)

TimeframeStudies, this research(%)All Research%
pre-199040 (33.33)18.7374
1990's27 (22.50)18.2507
2000's16 (13.33)29.6817
2010's30 (25.00)24.3611
2020's7 (5.83)2.80

Authors

AuthorsStudies
Iwatsubo, M; Labeyrie, F; Mével-Ninio, M1
Romslo, I; Ulvik, R1
Labeyrie, F; Mevel-Ninio, M; Risler, Y1
Centeno, F; Gutiérrez-Merino, C1
Kay, CJ; Lippay, EW1
Tollin, G; Walker, MC1
Neupert, W; Nicholson, DW1
Blankenship, RE; Cusanovich, MA; Freeman, JC; Meyer, TE; Tollin, G1
Desbois, A; Gervais, M; Lutz, M; Tegoni, M1
LeGall, J; Moura, I; Moura, JJ; Peck, HD; Stewart, DE; Wampler, JE; Weiner, PK; Xavier, AV1
Cusanovich, MA; Eltis, L; Hazzard, JT; Mauk, AG; Tollin, G1
Cusanovich, MA; Meyer, TE; Tollin, G; Vorkink, WP1
Crichton, RR; Funk, F; Lecrenier, C; Lesuisse, E; Schneider, W1
Masaki, R; Taketani, S; Tanaka-Yoshioka, A; Tashiro, Y; Tokunaga, R1
Green, BG; Kennedy, FS; Williams, DM1
Kamin, H; Murphy, MJ; Siegel, LM1
Coon, MJ; van der Hoeven, TA1
Chase, HP; Holtzman, J; Rumack, BH1
Bartsch, RG; Horio, T; Kakuno, T; Kamen, MD1
Ogura, Y; Suzuki, H2
Groudinsky, O; Risler, JL1
Nicholas, DJ; Prabhakararao, K1
Garland, PB; Ragan, CI1
Mével-Ninio, M1
Nishibayashi, H; Sato, R1
Bartsch, RG; Kamen, MD; Meyer, TE1
Oreland, L1
Risler, JL1
Labeyrie, F; Mevel-Ninio, M; Pajot, P1
Sturtevant, JM; Tsong, TY3
Ballot, B; Ignarro, LJ; Wolin, MS; Wood, KS1
Bonnett, R1
Kobayashi, K; Yoshimoto, A1
Holm, RH; Paech, C; Reynolds, JG; Singer, TP1
Ulvik, RJ1
Gervais, M; Labeyrie, F; Risler, Y; Vergnes, O1
Ghosh, DK; Stuehr, DJ1
Govindaraj, S; Poulos, TL1
Baek, KJ; Lucas, S; Stuehr, DJ; Thiel, BA1
Gonvindaraj, S; Li, H; Poulos, TL1
Hazzard, JT; McDonough, CA; Tollin, G1
Cambillau, C; Tegoni, M1
Abu-Soud, HM; Ghosh, DK; Siddhanta, U; Stuehr, DJ; Wu, C; Zhang, J1
Bächinger, HP; Glatter, O; Klatt, P; Lehner, D; List, BM; Mayer, B; Pfeiffer, S; Schmidt, K; Werner, ER1
Chapman, SK; Daff, S; Ingledew, WJ; Reid, GA1
Boyhan, A; Charles, I; Lowe, PN; Moncada, S; Riveros-Moreno, V; Smith, D; Stammers, DK1
Capeillere-Blandin, C; Lederer, F; Mayer, M; Rouviere-Fourmy, N; Tegoni, M1
Lé, KH; Lederer, F; Miles, CS1
Chapman, SK; Coggins, JR; Daff, S; Lindsay, JG; Munro, AW2
Bell, C; Chapman, SK; Daff, S; Reid, GA; Short, D1
Chapman, SK; Reid, GA; Sharp, RE1
Klatt, P; Mayer, B; Schmidt, K; Werner, ER1
Govindaraj, S; Hazzard, JT; Poulos, TL; Tollin, G1
Peterson, JA; Sevrioukova, I; Truan, G1
Chapman, SK; Daff, SN; Govindaraj, S; Holt, RA; Munro, AW; Poulos, TL; Turner, KL1
Hurshman, AR; Marletta, MA; Rusche, KM1
Andrew, PJ; Brunner, K; Hemmens, B; Kungl, AJ; Mayer, B; Tortschanoff, A1
Li, H; Peterson, JA; Poulos, TL; Sevrioukova, IF; Zhang, H1
Li, H; Poulos, TL1
Asano, Y; Kato, Y; Mayhew, SG; Nakamura, K; Sakiyama, H1
Chapman, SK; Cheesman, MR; Miles, CS; Mowat, CG; Munro, AW; Quaroni, LG; Reid, GA1
Davydov, D; Jung, C; Kariakin, A; Peterson, JA1
Asano, Y; Kato, Y1
FABRICANT, J; SMITH, SL; VANDEMARK, PJ1
MORTON, RK; STURTEVANT, JM1
BENZIMAN, M; GALANTER, Y1
LABEYRIE, F; SLONIMSKI, PP1
Enemark, JH; Feng, C; Ghosh, DK; Holliday, MA; Salerno, JC; Thomas, C; Tollin, G2
Higashimoto, Y; Noguchi, M; Palmer, G; Sakamoto, H; Sato, H; Takahashi, K1
Feng, C; Ghosh, DK; Guillemette, JG; Hazzard, JT; Nahm, NJ; Salerno, JC; Tollin, G1
Chen, B; Estabrook, RW; Haines, DC; Kitazume, T; Peterson, JA1
Aulak, KS; Panda, K; Stuehr, DJ; Tejero, J; Tiso, M1
Feng, C; Ghosh, DK; Hazzard, JT; Masters, BS; Roman, LJ; Tollin, G1
Dupont, AL; Feng, C; Ghosh, DK; Guillemette, JG; Hazzard, JT; Nahm, NJ; Spratt, DE; Tollin, G; Weinberg, JB1
Dupont, A; Elmore, BO; Feng, C; Ghosh, DK; Guillemette, JG; Kirk, ML; Sempombe, J; Sun, X1
Fadlalla, M; Haque, MM; Panda, K; Ray, SS; Stuehr, DJ; Wang, ZQ1
Haque, MM; Stuehr, DJ; Tejero, J1
Feng, C; Tollin, G1
Durra, D; Haque, MM; Stuehr, DJ; Tejero, J1
Hannibal, L; Mustovich, A; Stuehr, DJ; Tejero, J1
Astashkin, AV; Elmore, BO; Fan, W; Feng, C; Guillemette, JG1
Flück, CE; Mullis, PE; Pandey, AV1
Curtis, RA; Dunford, AJ; Ekanem, IS; Fisher, K; Girvan, HM; Joyce, MG; Leys, D; Munro, AW; Neeli, R; Voice, MW; Waltham, TN; Williams, P1
Dupont, A; Fan, W; Feng, C; Ghosh, DK; Guy Guillemette, J; Tollin, G1
Lederer, F1
Beliaev, AS; Bradley, J; Butt, JN; Clarke, TA; Edwards, MJ; Fredrickson, JK; Gates, AJ; Hall, A; Marshall, MJ; Reardon, CL; Richardson, DJ; Shi, L; Wang, Z; Watmough, NJ; White, GF; Zachara, JM1
Backes, WL; Huber Iii, WJ; Marohnic, CC; Martásek, P; Masters, BS; McCammon, K; Panda, SP; Patrick Connick, J; Reed, JR1
Elmore, BO; Fan, W; Feng, C; Li, W1
Feng, C; Ghosh, DK; Guillemette, JG; Taiakina, V; Tollin, G1
Maskin, SS; Mochaĭlo, IuA; Pchelintsev, KE; Ponomarev, EA; Strepetov, NN1
Chen, L; Fan, W; Feng, C; Li, W1
Maskin, SS; Petrov, VI; Ponomarev, ÉA; Strepetov, NN1
Chen, L; Elmore, BO; Fan, W; Feng, C; Guillemette, JG; Li, W; Piazza, M1
Astashkin, AV; Chen, L; Elmore, BO; Feng, C; Li, W; Lu, C; Rousseau, DL; Yeh, SR1
Hashimoto, K; Nakamura, R; Nealson, KH; Okamoto, A1
Roccatano, D; Schwaneberg, U; Verma, R1
Kulp, DW; Marletta, MA; Schief, WR; Smith, BC; Underbakke, ES1
Chen, L; Elmore, BO; Fan, W; Feng, C; Li, W; Sun, X1
Astashkin, AV; Chen, L; Feng, C; Li, W; Masters, BS; Panda, SP; Roman, LJ; Venkatakrishnan, P1
Hanein, D; Martásek, P; Masters, BS; Page, C; Roman, LJ; Swift, M; Volkmann, N; Xu, XP1
Feng, C; Guo, D; Lau, G; Sheng, Y; Zhong, L1
Afriat-Jurnou, L; Ahmed, FH; Carr, PD; Flanagan, J; Greening, C; Hong, NS; Jackson, CJ; Lee, BM; Mohamed, AE; Taylor, MC1
Holden, JK; Hollingsworth, SA; Li, H; Poulos, TL1
Denkhaus, L; Fisher, K; Hay, S; Lafite, P; Leys, D; Menon, BR; Munro, AW; Ortmayer, M; Rigby, SE; Scrutton, NS; Tralau, T1
Bayachou, M; Haque, MM; Kenney, CT; Stuehr, DJ; Tejero, J1
Feng, C; Li, J; Miao, Y; Sheng, Y; Wang, W; Zheng, H1
Dubey, KD; Shaik, S1
Feng, C; Li, J; Zheng, H3
Belsare, KD; Martinez, R; Ruff, AJ; Schwaneberg, U1
Higuchi, T; Hisamatsu, Y; Otani, K; Takase, H; Umezawa, N1
Bánó, G; Berta, M; Hovan, A; Miskovsky, P; Sedlák, E; Sedláková, D1
Feng, C; Hossan, MY; Jiang, T; Li, J; Thielges, MC; Tumbic, GW1
Chan, ACK; Do, LTM; McGregor, AK; Murphy, MEP; Saini, G; Schroeder, MD; Wolthers, KR1

Reviews

8 review(s) available for heme and flavin mononucleotide

ArticleYear
Oxygen activation and tetrapyrroles.
    Essays in biochemistry, 1981, Volume: 17

    Topics: Animals; Chlorophyll; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Female; Flavin Mononucleotide; Heme; Hemoglobins; Humans; Infant, Newborn; Iron; Jaundice, Neonatal; Microsomes, Liver; Models, Molecular; Myoglobin; Naphthalenes; Oxidation-Reduction; Oxygen; Oxygen Consumption; Photochemistry; Phototherapy; Porphyrins; Pregnancy; Pyrroles; Solubility; Spectrophotometry; Stereoisomerism; Tetrapyrroles; Tryptophan Oxygenase

1981
Flavocytochrome b2: an ideal model system for studying protein-mediated electron transfer.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Cytochrome c Group; Electron Transport; Flavin Mononucleotide; Heme; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Macromolecular Substances; Models, Structural; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae

1996
Catalysis by nitric oxide synthase.
    Current opinion in chemical biology, 1998, Volume: 2, Issue:5

    Topics: Antioxidants; Arginine; Biopterins; Catalysis; Citrulline; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Hydrogen Peroxide; Isoenzymes; Nitric Oxide; Nitric Oxide Synthase

1998
Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3).
    Biochimica et biophysica acta, 1999, Nov-23, Volume: 1441, Issue:2-3

    Topics: Bacillus megaterium; Bacterial Proteins; Crystallization; Cytochrome P-450 Enzyme System; Electron Transport; Fatty Acids; Flavin Mononucleotide; Heme; Mixed Function Oxygenases; Models, Molecular; Molecular Structure; Mutagenesis; NADPH-Ferrihemoprotein Reductase; Protein Conformation

1999
[MODE OF ACTION OF LACTATE DEHYDROGENASES LINKED TO FLAVIN AND CYTOCHROME SYSTEMS].
    Bulletin de la Societe de chimie biologique, 1964, Volume: 46

    Topics: Biochemical Phenomena; Biochemistry; Cobalt; Cytochromes; Edetic Acid; Electron Transport; Enzyme Inhibitors; Ferrocyanides; Flavin Mononucleotide; Flavins; Heme; Ions; L-Lactate Dehydrogenase; Lactate Dehydrogenases; Lactates; Manganese; Mitochondria; Mutation; Oxalates; Phosphates; Research; Spectrum Analysis; Yeasts; Zinc

1964
Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.
    The FEBS journal, 2009, Volume: 276, Issue:15

    Topics: Animals; Binding Sites; Dimerization; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavoproteins; Heme; Models, Molecular; Nitric Oxide Synthase; Oxidation-Reduction; Protein Conformation

2009
Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b (2).
    European biophysics journal : EBJ, 2011, Volume: 40, Issue:12

    Topics: Binding Sites; Catalysis; Cytochrome b Group; Cytochromes b5; Cytochromes c; Electron Transport; Flavin Mononucleotide; Flavins; Heme; Kinetics; Mitochondria; Models, Molecular; NADPH Oxidases; Osmolar Concentration; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Saccharomyces cerevisiae

2011
Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.
    Journal of inorganic biochemistry, 2014, Volume: 130

    Topics: Calmodulin; Electron Transport; Flavin Mononucleotide; Heme; Kinetics; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Nitric Oxide Synthase Type III

2014

Other Studies

112 other study(ies) available for heme and flavin mononucleotide

ArticleYear
Rapid kinetic studies of partial reactions in the heme free derivative of L-lactate cytochrome c oxidoreductase (flavocytochrome b2); the flavodehydrogenase function.
    Biochemistry, 1977, Aug-09, Volume: 16, Issue:16

    Topics: Apoenzymes; Cytochrome c Group; Electron Transport; Ferricyanides; Flavin Mononucleotide; Flavoproteins; Heme; Kinetics; L-Lactate Dehydrogenase; Mathematics; Oxidation-Reduction; Saccharomyces cerevisiae; Spectrophotometry; Spectrophotometry, Ultraviolet

1977
Studies on the utilization of ferritin iron in the ferrochelatase reaction of isolated rat liver mitochondria.
    Biochimica et biophysica acta, 1978, Jun-15, Volume: 541, Issue:2

    Topics: Animals; Cytosol; Deuterium; Ferritins; Ferrochelatase; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; In Vitro Techniques; Iron; Kinetics; Lyases; Lysosomes; Microsomes, Liver; Mitochondria, Liver; NAD; Rats; Succinates

1978
Structural studies of yeast flavocytochrome b2: cooperative roles of the alpha and beta globules in the formation of the flavin-binding sites.
    European journal of biochemistry, 1977, Feb-15, Volume: 73, Issue:1

    Topics: Binding Sites; Chromatography, Gel; Cytochromes; Flavin Mononucleotide; Flavoproteins; Guanidines; Heme; Macromolecular Substances; Molecular Conformation; Molecular Weight; Protein Binding; Protein Denaturation

1977
Location of functional centers in the microsomal cytochrome P450 system.
    Biochemistry, 1992, Sep-15, Volume: 31, Issue:36

    Topics: Animals; Binding Sites; Coumarins; Cytochrome P-450 Enzyme System; Energy Metabolism; Energy Transfer; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Fluorescence; Heme; Lipids; Microsomes, Liver; NADPH-Ferrihemoprotein Reductase; Protein Conformation; Rats; Water

1992
Mutation of the heme-binding crevice of flavocytochrome b2 from Saccharomyces cerevisiae: altered heme potential and absence of redox cooperativity between heme and FMN centers.
    Biochemistry, 1992, Nov-24, Volume: 31, Issue:46

    Topics: Base Sequence; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Molecular Sequence Data; Mutation; Oligonucleotides; Oxidation-Reduction; Potentiometry; Saccharomyces cerevisiae; Thermodynamics

1992
Laser flash photolysis study of the kinetics of electron transfer reactions of flavocytochrome b2 from Hansenula anomala: further evidence for intramolecular electron transfer mediated by ligand binding.
    Biochemistry, 1992, Mar-17, Volume: 31, Issue:10

    Topics: Electron Transport; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lasers; Ligands; Oxidation-Reduction; Photolysis; Pichia; Pyruvates; Saccharomyces cerevisiae

1992
Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c.
    Proceedings of the National Academy of Sciences of the United States of America, 1989, Volume: 86, Issue:12

    Topics: Apoproteins; Cytochrome c Group; Cytochromes c; Dithionite; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Lyases; Mitochondria; NAD; Oxidation-Reduction; Saccharomyces cerevisiae

1989
In vitro kinetics of reduction of cytochrome c554 isolated from the reaction center of the green phototrophic bacterium, Chloroflexus aurantiacus.
    Archives of biochemistry and biophysics, 1989, Volume: 272, Issue:1

    Topics: Bacteria; Bacterial Proteins; Cytochrome c Group; Flavin Mononucleotide; Flavins; Heme; Kinetics; Osmolar Concentration; Oxidation-Reduction; Photolysis; Photosynthetic Reaction Center Complex Proteins

1989
Flavin and heme structures in lactate:cytochrome c oxidoreductase: a resonance Raman study.
    Biochemistry, 1989, Oct-03, Volume: 28, Issue:20

    Topics: Flavin Mononucleotide; Heme; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Oxidation-Reduction; Protoporphyrins; Spectrum Analysis, Raman

1989
A hypothetical model of the flavodoxin-tetraheme cytochrome c3 complex of sulfate-reducing bacteria.
    Biochemistry, 1988, Apr-05, Volume: 27, Issue:7

    Topics: Cytochrome c Group; Desulfovibrio; Flavin Mononucleotide; Flavodoxin; Flavoproteins; Heme; Kinetics; Models, Molecular; Protein Conformation

1988
Kinetics of flavin semiquinone reduction of the components of the cytochrome c-cytochrome b5 complex.
    Biochemistry, 1988, Jul-26, Volume: 27, Issue:15

    Topics: Animals; Cytochrome b Group; Cytochrome c Group; Cytochromes b5; Flavin Mononucleotide; Flavins; Heme; In Vitro Techniques; Kinetics; Oxidation-Reduction; Peptide Fragments; Quinones

1988
Chromatium flavocytochrome c: kinetics of reduction of the heme subunit, and the flavocytochrome c-mitochondrial cytochrome c complex.
    Archives of biochemistry and biophysics, 1985, Volume: 236, Issue:1

    Topics: Animals; Bacteria; Carbon Monoxide; Chromatium; Chromatography, Gel; Cytochrome c Group; Flavin Mononucleotide; Flavins; Heme; Horses; Mitochondria, Heart; Oxidation-Reduction; Protein Binding; Spectrophotometry

1985
A comparative study on iron sources for mitochondrial haem synthesis including ferritin and models of transit pool species.
    European journal of biochemistry, 1986, Jun-02, Volume: 157, Issue:2

    Topics: Animals; Electron Transport Complex IV; Ferritins; Ferrozine; Flavin Mononucleotide; Heme; Horses; Iron; Kinetics; Mitochondria, Liver; Models, Chemical; Monoamine Oxidase; Phenanthrolines; Rats; Rats, Inbred Strains; Spleen

1986
Association of ferrochelatase with Complex I in bovine heart mitochondria.
    Biochimica et biophysica acta, 1986, Sep-04, Volume: 883, Issue:2

    Topics: Animals; Cardiolipins; Cattle; Ferrochelatase; Flavin Mononucleotide; Heme; Immunosorbent Techniques; Lyases; Mitochondria, Heart; NAD; NAD(P)H Dehydrogenase (Quinone); Oxidation-Reduction; Phosphatidylserines; Quinone Reductases

1986
The effect of iron substrate on mitochondrial haem synthesis in copper deficiency.
    The British journal of nutrition, 1985, Volume: 53, Issue:1

    Topics: Animals; Copper; Ferritins; Flavin Mononucleotide; Heme; In Vitro Techniques; Iron; Liver; Male; Mitochondria, Liver; Rats; Rats, Inbred Strains

1985
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups.
    The Journal of biological chemistry, 1973, Jan-10, Volume: 248, Issue:1

    Topics: Amino Acids; Ammonium Sulfate; Chemical Precipitation; Chromatography, Gel; Chromatography, Thin Layer; Electron Spin Resonance Spectroscopy; Electrophoresis, Disc; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Immunoelectrophoresis; Iron; Ligands; Molecular Weight; NADH, NADPH Oxidoreductases; NADP; Oxidoreductases; Spectrophotometry; Sulfides; Sulfites; Ultracentrifugation

1973
Preparation and properties of partially purified cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase from rabbit liver microsomes.
    The Journal of biological chemistry, 1974, Oct-10, Volume: 249, Issue:19

    Topics: Animals; Binding Sites; Carbon Monoxide; Centrifugation, Density Gradient; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Detergents; Dithionite; Electrophoresis, Disc; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Male; Microsomes, Liver; Mixed Function Oxygenases; Molecular Weight; NADP; Oxidation-Reduction; Phospholipids; Polyethylene Glycols; Protein Binding; Rabbits; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfides

1974
Hepatic drug metabolism and protein malnutrition.
    The Journal of pharmacology and experimental therapeutics, 1973, Volume: 186, Issue:3

    Topics: Aniline Compounds; Animals; Body Weight; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Cytochromes; Dietary Proteins; Female; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Haplorhini; Heme; Kinetics; Liver; Macaca; Methyltransferases; Microsomes, Liver; Mixed Function Oxygenases; Morphinans; Organ Size; Phospholipids; Protein Deficiency; Riboflavin

1973
Two reduced nicotinamide adenine dinucleotide dehydrogenases from the photosynthetic bacterium, Rhodospirillum rubrum.
    The Journal of biological chemistry, 1969, Nov-10, Volume: 244, Issue:21

    Topics: Bacterial Chromatophores; Bacterial Proteins; Chemical Phenomena; Chemistry; Drug Stability; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Hydrogen-Ion Concentration; Imines; Light; Methods; Models, Biological; Molecular Weight; NAD; Oxidoreductases; Photosynthesis; Quinones; Radiation Effects; Rhodospirillum

1969
The kinetic behavior of the FMN and protoheme moieties of yeast L(plus)-lactate dehydrogenase (cytochrome b2).
    Journal of biochemistry, 1970, Volume: 67, Issue:2

    Topics: Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; Oxidation-Reduction; Spectrophotometry; Yeasts

1970
Magnetic-circular-dichroism studies of cytochrome c and cytochrome b 2 .
    European journal of biochemistry, 1973, Volume: 35, Issue:2

    Topics: Animals; Apoproteins; Circular Dichroism; Cytochrome c Group; Cytochromes; Flavin Mononucleotide; Heme; Horses; L-Lactate Dehydrogenase; Magnetic Resonance Spectroscopy; Magnetics; Myocardium; Protein Conformation

1973
Sulphite reductase from bakers' yeast: a haemoflavoprotein.
    Biochimica et biophysica acta, 1969, Jun-24, Volume: 180, Issue:2

    Topics: Benzoates; Carbon Monoxide; Cell-Free System; Chromatography, Gel; Chromatography, Ion Exchange; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Heme; Kinetics; Light; Methods; NADP; Nitrobenzenes; Oxidoreductases; Plant Proteins; Riboflavin; Saccharomyces; Spectrum Analysis; Sulfites; Sulfur Isotopes

1969
Spectroscopic studies of flavoproteins and non-haem iron proteins of submitochondrial particles of Torulopsis utilis modified by iron- and sulphate-limited growth in continuous culture.
    The Biochemical journal, 1971, Volume: 124, Issue:1

    Topics: Cycloheximide; Cytochromes; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavoproteins; Glycerolphosphate Dehydrogenase; Heme; Iron; Mitochondria; Mitosporic Fungi; NAD; NADP; Oxidation-Reduction; Oxidoreductases; Proteins; Spectrum Analysis; Succinate Dehydrogenase; Sulfates; Sulfides; Ubiquinone

1971
Subunit structure of L-lactate dehydrogenase (cytochrome b2) of Saccharomyces cerevisiae. Ultracentrifugation studies.
    European journal of biochemistry, 1972, Feb-15, Volume: 25, Issue:2

    Topics: Chromatography, Gel; Cytochromes; Flavin Mononucleotide; Flavins; Guanidines; Heme; L-Lactate Dehydrogenase; Macromolecular Substances; Molecular Weight; Protein Conformation; Saccharomyces; Saccharomyces cerevisiae; Ultracentrifugation

1972
Preparation of hepatic microsomal particles containing P-450 as the sole heme constituent and absolute spectra of P-450.
    Journal of biochemistry, 1968, Volume: 63, Issue:6

    Topics: Animals; Bacillus subtilis; Chemical Phenomena; Chemistry, Physical; Cytochromes; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Glycerol; Heme; Liver; Microsomes; Peptide Hydrolases; Pigments, Biological; Proteins; Rabbits; Spectrophotometry; Spectrum Analysis; Trypsin

1968
Cytochrome c 3 . A class of electron transfer heme proteins found in both photosynthetic and sulfate-reducing bacteria.
    Biochimica et biophysica acta, 1971, Sep-07, Volume: 245, Issue:2

    Topics: Amino Acids; Ammonium Sulfate; Bacteria; Chemical Phenomena; Chemical Precipitation; Chemistry, Physical; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cyanobacteria; Cytochromes; Desulfovibrio; Electrophoresis; Flavin Mononucleotide; Heme; Molecular Weight; Oxidation-Reduction; Photosynthesis; Rhodopseudomonas; Species Specificity; Spectrophotometry; Sulfites; Ultracentrifugation

1971
Purification and properties of pig liver mitochondrial monoamine oxidase.
    Archives of biochemistry and biophysics, 1971, Volume: 146, Issue:2

    Topics: Amino Acids; Animals; Centrifugation, Density Gradient; Chromatography, Gel; Chromatography, Paper; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Hexosamines; Hydrogen-Ion Concentration; Kinetics; Mitochondria, Liver; Molecular Weight; Monoamine Oxidase; Neuraminic Acids; Swine

1971
Effect of pH on the kinetic parameters of yeast L(plus)-lactate dehydrogenase (cytochrome b2).
    Journal of biochemistry, 1970, Volume: 67, Issue:2

    Topics: Cytochromes; Electron Transport; Ferricyanides; Flavin Mononucleotide; Heme; Hydrogen-Ion Concentration; Kinetics; L-Lactate Dehydrogenase; Oxidation-Reduction; Spectrophotometry; Yeasts

1970
Fluorescence and phosphorescence of yeast L-lactate dehydrogenase (cytochrome b2). Relative orientations of the prosthetic heme and flavin.
    Biochemistry, 1971, Jul-06, Volume: 10, Issue:14

    Topics: Chemical Phenomena; Chemistry; Cytochromes; Energy Transfer; Flavin Mononucleotide; Fluorescence; Fluorometry; Heme; L-Lactate Dehydrogenase; Luminescent Measurements; Mathematics; Models, Structural; Porphyrins; Protein Binding; Saccharomyces; Temperature; Tryptophan

1971
Reconstitution of cytochrome b2 following prosthetic groups dissociation by guanidine hydrochloride, Protoheme binding.
    Biochimie, 1971, Volume: 53, Issue:1

    Topics: Binding Sites; Chemical Phenomena; Chemistry; Cytochromes; Flavin Mononucleotide; Guanidines; Heme; Spectrophotometry; Spectrum Analysis

1971
Investigations of yeast L-lactate dehydrogenase (cytochrome b2). IV. Optical rotatory dispersion.
    The Journal of biological chemistry, 1968, May-10, Volume: 243, Issue:9

    Topics: Flavin Mononucleotide; Heme; Hydrogen; L-Lactate Dehydrogenase; Lactates; Mercaptoethanol; Mercury; Optical Rotatory Dispersion; Platinum; Saccharomyces; Sulfonic Acids

1968
Investigations of yeast L-lactate dehydrogenase (cytochrome b2). V. Circular dichroism of the flavin mononucleotide-free apoenzyme.
    The Journal of biological chemistry, 1969, May-10, Volume: 244, Issue:9

    Topics: Cytochromes; Drug Storage; Flavin Mononucleotide; Heme; L-Lactate Dehydrogenase; Mercaptoethanol; Oxidation-Reduction; Protein Denaturation; Saccharomyces; Spectrophotometry; Spectrum Analysis; Sulfonic Acids

1969
Investigations of yeast L-lactate dehydrogenase (cytochrome b2). VI. Circular dichroism of the holoenzyme.
    The Journal of biological chemistry, 1969, Sep-25, Volume: 244, Issue:18

    Topics: Ascomycota; Chemical Phenomena; Chemistry; Crystallization; Cytochromes; DNA; Flavin Mononucleotide; Heme; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Mathematics; Optical Rotatory Dispersion; Peptides; Saccharomyces; Spectrophotometry; Spectrum Analysis; Urea

1969
Guanylate cyclase from bovine lung. Evidence that enzyme activation by phenylhydrazine is mediated by iron-phenyl hemoprotein complexes.
    The Journal of biological chemistry, 1984, May-10, Volume: 259, Issue:9

    Topics: Animals; Cattle; Enzyme Activation; Flavin Mononucleotide; Guanylate Cyclase; Heme; Hemeproteins; Iron; Kinetics; Lung; Molecular Weight; Nitric Oxide; Phenylhydrazines; Potassium Cyanide; Protein Binding

1984
Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics.
    Biochimica et biophysica acta, 1982, Aug-10, Volume: 705, Issue:3

    Topics: Amino Acids; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Macromolecular Substances; Molecular Weight; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Conformation; Saccharomyces cerevisiae

1982
Structural identification of iron-sulfur clusters of the respiratory chain-linked NADH dehydrogenase.
    The Journal of biological chemistry, 1981, Apr-10, Volume: 256, Issue:7

    Topics: Anaerobiosis; Animals; Cattle; Cytochrome Reductases; Flavin Mononucleotide; Fourier Analysis; Heme; Iron; Iron-Sulfur Proteins; Macromolecular Substances; Magnetic Resonance Spectroscopy; Metalloproteins; Mitochondria, Heart; NADH Dehydrogenase; Protein Conformation; Spectrophotometry; Sulfur

1981
Ferritin iron as substrate for synthesis of protoheme in intact rat liver mitochondria.
    FEBS letters, 1981, Sep-28, Volume: 132, Issue:2

    Topics: Animals; Ferritins; Flavin Mononucleotide; Heme; Iron; Kinetics; Membrane Potentials; Mitochondria, Liver; Oxidative Phosphorylation; Phenanthrolines; Protoporphyrins; Rats

1981
A flavin-mononucleotide-binding site in Hansenula anomala nicked flavocytochrome b2, requiring the association of two domains.
    European journal of biochemistry, 1980, Volume: 111, Issue:1

    Topics: Ascomycota; Binding Sites; Flavin Mononucleotide; Heme; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Molecular Weight; Peptide Fragments; Pichia; Protein Binding; Trypsin

1980
Macrophage NO synthase: characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction.
    Biochemistry, 1995, Jan-24, Volume: 34, Issue:3

    Topics: Amino Acid Oxidoreductases; Amino Acid Sequence; Animals; Biopterins; Calmodulin; Catalysis; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Macrophages; Mice; Molecular Sequence Data; Molecular Weight; Nitric Oxide Synthase; Peptide Fragments; Protein Conformation; Spectrum Analysis; Structure-Activity Relationship; Trypsin

1995
Role of the linker region connecting the reductase and heme domains in cytochrome P450BM-3.
    Biochemistry, 1995, Sep-05, Volume: 34, Issue:35

    Topics: Amino Acid Sequence; Bacillus megaterium; Bacterial Proteins; Binding Sites; Cytochrome P-450 Enzyme System; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Hydroxylation; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Myristic Acid; Myristic Acids; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Sequence Deletion; Sequence Homology, Amino Acid

1995
Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme.
    The Journal of biological chemistry, 1993, Oct-05, Volume: 268, Issue:28

    Topics: Amino Acid Oxidoreductases; Animals; Biopterins; Catalysis; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Macrophages; Mice; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxidoreductases; Substrate Specificity

1993
Flavin supported fatty acid oxidation by the heme domain of Bacillus megaterium cytochrome P450BM-3.
    Biochemical and biophysical research communications, 1994, Sep-30, Volume: 203, Issue:3

    Topics: Bacillus megaterium; Bacterial Proteins; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Heme; Mixed Function Oxygenases; Myristic Acid; Myristic Acids; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Radioisotope Dilution Technique; Spectrophotometry

1994
Intramolecular electron transfer in yeast flavocytochrome b2 upon one-electron photooxidation of the fully reduced enzyme: evidence for redox state control of heme-flavin communication.
    Biochemistry, 1994, Nov-15, Volume: 33, Issue:45

    Topics: Electron Transport; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; Oxidation-Reduction; Saccharomyces cerevisiae; Spectrum Analysis

1994
The 2.6-A refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex.
    Protein science : a publication of the Protein Society, 1994, Volume: 3, Issue:2

    Topics: Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli; Flavin Mononucleotide; Heme; Hydrogen Bonding; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Macromolecular Substances; Molecular Structure; Molecular Weight; Recombinant Proteins; Saccharomyces cerevisiae; Sulfites

1994
Heme iron reduction and catalysis by a nitric oxide synthase heterodimer containing one reductase and two oxygenase domains.
    The Journal of biological chemistry, 1996, Mar-29, Volume: 271, Issue:13

    Topics: Animals; Binding Sites; Calmodulin; Catalysis; Cell Line; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Iron; Kinetics; Macromolecular Substances; Macrophages; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxidoreductases; Oxygenases; Spectrophotometry

1996
Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin.
    The Journal of biological chemistry, 1996, Mar-29, Volume: 271, Issue:13

    Topics: Animals; Arginine; Binding Sites; Biopterins; Brain; Chromatography, Gel; Circular Dichroism; Citrulline; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Isoenzymes; Light; Macromolecular Substances; Neurons; Nitric Oxide Synthase; Nitroarginine; Protein Conformation; Protein Structure, Secondary; Rats; Scattering, Radiation; Thermodynamics

1996
New insights into the catalytic cycle of flavocytochrome b2.
    Biochemistry, 1996, May-21, Volume: 35, Issue:20

    Topics: Catalysis; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Inhibitors; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Mitochondria; Models, Biological; Oxidation-Reduction; Pyruvates; Pyruvic Acid; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry

1996
Identification of the domains of neuronal nitric oxide synthase by limited proteolysis.
    The Biochemical journal, 1996, Feb-15, Volume: 314 ( Pt 1)

    Topics: Amino Acid Sequence; Animals; Arginine; Binding Sites; Biopterins; Blotting, Western; Brain; Calmodulin; Chymotrypsin; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Heme; Humans; Molecular Sequence Data; Molecular Weight; Nitric Oxide Synthase; Nitroarginine; Peptide Fragments; Rabbits; Rats; Recombinant Proteins; Trypsin

1996
On the molecular basis of inhibition by excess substrate in wild-type and Y143F flavocytochrome b2.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Acetates; Binding Sites; Cytochrome c Group; Flavin Mononucleotide; Heme; Homeostasis; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactates; Point Mutation

1996
Functional uncoupling between flavin and heme domains in flavocytochrome b2 by a monoclonal antibody.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Antibodies, Monoclonal; Binding Sites; Enzyme-Linked Immunosorbent Assay; Epitopes; Flavin Mononucleotide; Heme; Immunoglobulin G; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Saccharomyces cerevisiae

1996
Formation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Guanidine; Guanidines; Heme; Kinetics; Mixed Function Oxygenases; NAD; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Quinones; Spectrophotometry

1996
Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region.
    The Biochemical journal, 1996, Jun-01, Volume: 316 ( Pt 2)

    Topics: Amino Acid Sequence; Base Sequence; Catalysis; DNA Primers; Electron Transport; Escherichia coli; Ferricyanides; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactates; Lactic Acid; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Saccharomyces cerevisiae

1996
Probing electron transfer in flavocytochrome P-450 BM3 and its component domains.
    European journal of biochemistry, 1996, Jul-15, Volume: 239, Issue:2

    Topics: Bacillus megaterium; Bacterial Proteins; Binding Sites; Cloning, Molecular; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Peptide Fragments; Quinones; Recombinant Proteins; Restriction Mapping

1996
Determination of nitric oxide synthase cofactors: heme, FAD, FMN, and tetrahydrobiopterin.
    Methods in enzymology, 1996, Volume: 268

    Topics: Animals; Baculoviridae; Biopterins; Brain; Cell Line; Chromatography, High Pressure Liquid; Coenzymes; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Nitric Oxide Synthase; Rats; Recombinant Proteins; Spectrophotometry; Spodoptera; Transfection

1996
Electron transfer between the FMN and heme domains of cytochrome P450BM-3. Effects of substrate and CO.
    The Journal of biological chemistry, 1997, Mar-21, Volume: 272, Issue:12

    Topics: Bacterial Proteins; Cytochrome P-450 Enzyme System; Electron Transport; Flavin Mononucleotide; Heme; Kinetics; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Riboflavin; Spectrum Analysis; Substrate Specificity

1997
Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains.
    Archives of biochemistry and biophysics, 1997, Apr-15, Volume: 340, Issue:2

    Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Heme; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Palmitic Acid; Protein Binding; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Substrate Specificity

1997
Redox control of the catalytic cycle of flavocytochrome P-450 BM3.
    Biochemistry, 1997, Nov-11, Volume: 36, Issue:45

    Topics: Bacillus megaterium; Bacterial Proteins; Catalysis; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavoproteins; Heme; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Potentiometry; Protein Structure, Tertiary

1997
Sensitivity of flavin fluorescence dynamics in neuronal nitric oxide synthase to cofactor-induced conformational changes and dimerization.
    Biochemistry, 1998, Dec-15, Volume: 37, Issue:50

    Topics: Animals; Arginine; Biopterins; Brain; Calmodulin; Dimerization; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorescence Polarization; Heme; Holoenzymes; Nerve Tissue Proteins; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Protein Binding; Protein Conformation; Rats; Spectrometry, Fluorescence; Substrate Specificity; Thermodynamics

1998
Structure of a cytochrome P450-redox partner electron-transfer complex.
    Proceedings of the National Academy of Sciences of the United States of America, 1999, Mar-02, Volume: 96, Issue:5

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electron Transport; Flavin Mononucleotide; Flavodoxin; Heme; Mixed Function Oxygenases; Models, Molecular; Molecular Sequence Data; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Structure, Secondary; Recombinant Proteins; Static Electricity

1999
Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene.
    Biochemistry, 2000, Feb-01, Volume: 39, Issue:4

    Topics: Amino Acid Sequence; Bacillus; Bacterial Proteins; Cloning, Molecular; Enzyme Activation; Enzyme Stability; Escherichia coli; Flavin Mononucleotide; Gene Expression Regulation, Bacterial; Genes, Bacterial; Heme; Hydrogen-Ion Concentration; Kinetics; Lyases; Molecular Sequence Data; Spectrophotometry; Substrate Specificity; Temperature

2000
Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2000, Volume: 5, Issue:5

    Topics: Amino Acid Substitution; Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Heme; Histidine; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Mutation; Oxidation-Reduction; Protein Binding; Saccharomyces cerevisiae; Spectrophotometry; Spectrum Analysis, Raman

2000
A new approach to the study of protein-protein interaction by FTIR: complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain.
    Biochemistry, 2002, Nov-19, Volume: 41, Issue:46

    Topics: Bacillus megaterium; Bacterial Proteins; Binding Sites; Cytochrome P-450 Enzyme System; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorescent Dyes; Heme; Humans; Microsomes; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Osmolar Concentration; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared

2002
High-level expression of a novel FMN-dependent heme-containing lyase, phenylacetaldoxime dehydratase of Bacillus sp. strain OxB-1, in heterologous hosts.
    Protein expression and purification, 2003, Volume: 28, Issue:1

    Topics: Bacillus; Bacterial Proteins; Culture Media; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin Mononucleotide; Gene Expression; Heme; Lyases; Recombinant Proteins; Temperature

2003
RESPIRATORY PATHWAYS IN THE MYCOPLASMA. I. LACTATE OXIDATION BY MYCOPLASMA GALLISEPTICUM.
    Journal of bacteriology, 1963, Volume: 86

    Topics: Adenine Nucleotides; Diphosphates; Electron Transport; Flavin Mononucleotide; Flavins; Heme; Lactates; Lactic Acid; Metabolism; Mycoplasma; Mycoplasma gallisepticum; Mycoplasma Infections; NAD; NADH, NADPH Oxidoreductases; Nucleotides; Oxidation-Reduction; Oxidoreductases; Research

1963
KINETIC INVESTIGATIONS OF YEAST L-LACTATE DEHYDROGENASE (CYTOCHROME B2). I. THE DEHYDROGENATION OF L-LACTATE IN THE PRESENCE AND ABSENCE OF FERRICYANIDE AS ELECTRON ACCEPTOR.
    The Journal of biological chemistry, 1964, Volume: 239

    Topics: Catalysis; Cytochromes; Electrons; Ferricyanides; Ferrocyanides; Flavin Mononucleotide; Heme; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactates; Lactic Acid; Oxidation-Reduction; Research; Saccharomyces

1964
FLAVINE ADENINE DINUCLEOTIDE-LINKED MALIC DEHYDROGENASE FROM ACETOBACTER XYLINUM.
    Journal of bacteriology, 1964, Volume: 88

    Topics: Acetobacter; Adenine; Amobarbital; Enzyme Inhibitors; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Gluconacetobacter xylinus; Heme; Imidazoles; Iron; Israel; Malate Dehydrogenase; Malates; Pharmacology; Phenanthrolines; Phenazines; Phenols; Quinacrine; Quinolines; Research; Riboflavin

1964
Direct measurement by laser flash photolysis of intramolecular electron transfer in a two-domain construct of murine inducible nitric oxide synthase.
    Journal of the American Chemical Society, 2006, Mar-22, Volume: 128, Issue:11

    Topics: Animals; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Mice; NADP; Nitric Oxide Synthase Type II; Oxidation-Reduction; Photolysis; Protein Structure, Tertiary

2006
Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: the output state in nitric oxide formation.
    Biochemistry, 2006, May-23, Volume: 45, Issue:20

    Topics: Animals; Benzoquinones; Calmodulin; Electron Transport; Enzyme Activation; Flavin Mononucleotide; Heme; Heme Oxygenase (Decyclizing); Kinetics; Lasers; Models, Biological; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Photochemistry; Photolysis; Protein Structure, Tertiary; Rats; Recombinant Fusion Proteins; Riboflavin

2006
The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN.
    The Journal of biological chemistry, 2006, Oct-20, Volume: 281, Issue:42

    Topics: Animals; Binding Sites; Deferoxamine; Ferricyanides; Flavin Mononucleotide; Heme; Heme Oxygenase-1; Humans; Models, Chemical; Models, Molecular; Mutation; NADPH-Ferrihemoprotein Reductase; Rats

2006
Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase.
    Journal of the American Chemical Society, 2007, May-02, Volume: 129, Issue:17

    Topics: Animals; Calmodulin; Cloning, Molecular; Electrons; Escherichia coli; Flavin Mononucleotide; Heme; Kinetics; Lasers; Nitric Oxide Synthase Type I; Oxidation-Reduction; Photochemistry; Photolysis; Rats; Reverse Transcriptase Polymerase Chain Reaction; Riboflavin

2007
Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3.
    Biochemistry, 2007, Oct-23, Volume: 46, Issue:42

    Topics: Amino Acid Sequence; Bacillus megaterium; Bacterial Proteins; Buffers; Chromatography, Gel; Cytochrome P-450 Enzyme System; Dimerization; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Hydrogen-Ion Concentration; Mixed Function Oxygenases; Models, Chemical; Molecular Sequence Data; Molecular Weight; Mutation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen Consumption; Phosphates; Protein Structure, Tertiary; Sequence Homology, Amino Acid

2007
Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail.
    Biochemistry, 2007, Dec-18, Volume: 46, Issue:50

    Topics: Amino Acid Sequence; Animals; Computer Simulation; Cytochrome Reductases; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Molecular Sequence Data; Mutation; NADP; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Rats

2007
Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase.
    FEBS letters, 2008, Aug-06, Volume: 582, Issue:18

    Topics: Animals; Calmodulin; Electron Transport; Flavin Mononucleotide; Heme; Homeostasis; INDEL Mutation; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Photolysis; Protein Structure, Tertiary; Rats

2008
Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009, Volume: 14, Issue:1

    Topics: Animals; Benzoquinones; Electron Transport; Flavin Mononucleotide; Heme; Holoenzymes; Humans; Kinetics; Mice; Nitric Oxide; Nitric Oxide Synthase Type II; Oxidation-Reduction; Photochemistry; Time Factors

2009
Mutations in the FMN domain modulate MCD spectra of the heme site in the oxygenase domain of inducible nitric oxide synthase.
    Journal of the American Chemical Society, 2009, May-27, Volume: 131, Issue:20

    Topics: Binding Sites; Circular Dichroism; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Heme; Humans; Mutation; Nitric Oxide Synthase Type II; Protein Structure, Tertiary

2009
Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex.
    The Journal of biological chemistry, 2009, Jul-17, Volume: 284, Issue:29

    Topics: Binding Sites; Calmodulin; Catalysis; Ferrous Compounds; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Mutant Proteins; NADP; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Oxygen; Point Mutation; Temperature; Time Factors

2009
Regulation of interdomain electron transfer in the NOS output state for NO production.
    Dalton transactions (Cambridge, England : 2003), 2009, Sep-14, Issue:34

    Topics: Calmodulin; Electron Transport; Flavin Mononucleotide; Heme; Kinetics; Nitric Oxide; Nitric Oxide Synthase; Protein Isoforms; Protein Structure, Tertiary

2009
A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism.
    The Journal of biological chemistry, 2010, Aug-20, Volume: 285, Issue:34

    Topics: Animals; Binding Sites; Calmodulin; Catalysis; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Mutagenesis, Site-Directed; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Protein Structure, Tertiary; Rats

2010
Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.
    The Journal of biological chemistry, 2010, Aug-27, Volume: 285, Issue:35

    Topics: Animals; Catalysis; Electron Transport; Flavin Mononucleotide; Heme; Mice; Models, Chemical; Mutation; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Oxygen; Protein Structure, Tertiary; Rats; Surface Properties

2010
Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase.
    Journal of the American Chemical Society, 2010, Sep-01, Volume: 132, Issue:34

    Topics: Arginine; Biocatalysis; Electron Spin Resonance Spectroscopy; Electron Transport; Ferric Compounds; Flavin Mononucleotide; Heme; Humans; Nitric Oxide; Nitric Oxide Synthase Type II

2010
Altered heme catabolism by heme oxygenase-1 caused by mutations in human NADPH cytochrome P450 reductase.
    Biochemical and biophysical research communications, 2010, Sep-24, Volume: 400, Issue:3

    Topics: Adrenal Hyperplasia, Congenital; Alleles; Flavin Mononucleotide; Heme; Heme Oxygenase-1; Humans; Mutation; NADPH-Ferrihemoprotein Reductase; Polymorphism, Genetic; Protein Structure, Tertiary

2010
Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer.
    Archives of biochemistry and biophysics, 2011, Mar-01, Volume: 507, Issue:1

    Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Electron Transport; Fatty Acids; Flavin Mononucleotide; Heme; Hydroxylation; Mutation; NAD; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Multimerization

2011
Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin.
    FEBS letters, 2010, Oct-22, Volume: 584, Issue:20

    Topics: Binding Sites; Calcium; Calmodulin; Chelating Agents; Cloning, Molecular; Edetic Acid; Electron Transport; Flavin Mononucleotide; Heme; Heme Oxygenase (Decyclizing); Humans; Kinetics; Models, Biological; Nitric Acid; Nitric Oxide Synthase Type II; Oxidation-Reduction; Photochemistry; Photolysis

2010
Structure of a bacterial cell surface decaheme electron conduit.
    Proceedings of the National Academy of Sciences of the United States of America, 2011, Jun-07, Volume: 108, Issue:23

    Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Binding Sites; Crystallography, X-Ray; Cysteine; Cytochrome c Group; Cytochromes; Disulfides; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Heme; Iron; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Potentiometry; Protein Binding; Protein Structure, Tertiary; Shewanella

2011
Mutations of human cytochrome P450 reductase differentially modulate heme oxygenase-1 activity and oligomerization.
    Archives of biochemistry and biophysics, 2011, Sep-01, Volume: 513, Issue:1

    Topics: Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Heme Oxygenase-1; Humans; Multienzyme Complexes; Mutation, Missense; NADPH-Ferrihemoprotein Reductase; Oxidoreductases Acting on CH-CH Group Donors; Protein Multimerization

2011
Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase.
    FEBS letters, 2011, Aug-19, Volume: 585, Issue:16

    Topics: Buffers; Electron Transport; Ethylene Glycol; Flavin Mononucleotide; Heme; Humans; Kinetics; Nitric Oxide Synthase Type II; Protein Conformation; Protein Structure, Tertiary; Solutions; Spectrometry, Fluorescence; Sucrose; Viscosity

2011
Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme.
    Biochimica et biophysica acta, 2011, Volume: 1814, Issue:12

    Topics: Animals; Cattle; Electron Transport; Flavin Mononucleotide; Heme; Holoenzymes; Isoenzymes; Models, Biological; Nitric Oxide Synthase Type III; Photochemical Processes; Photolysis; Protein Structure, Tertiary; X-Ray Absorption Spectroscopy

2011
[Pharmacologic neuroprotection of the brain in carotid artery surgeries].
    Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 2011, Volume: 111, Issue:6

    Topics: Aged; Brain; Carotid Arteries; Carotid Stenosis; Drug Combinations; Endarterectomy, Carotid; Female; Flavin Mononucleotide; Heme; Humans; Hypoxia-Ischemia, Brain; Inosine Diphosphate; Male; Middle Aged; Neuroprotective Agents; Niacinamide; Reperfusion Injury; Succinates

2011
Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins.
    FEBS letters, 2012, Jan-20, Volume: 586, Issue:2

    Topics: Binding Sites; Electron Transport; Flavin Mononucleotide; Heme; Humans; In Vitro Techniques; Isoenzymes; Models, Biological; Models, Theoretical; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Binding; Protein Interaction Domains and Motifs; Temperature; Thermodynamics

2012
[Pharmacological neuroprotection against brain damage in ischemiai/reperfusion experiment].
    Eksperimental'naia i klinicheskaia farmakologiia, 2011, Volume: 74, Issue:8

    Topics: Animals; Brain; Drug Combinations; Drug Evaluation, Preclinical; Eosine Yellowish-(YS); Flavin Mononucleotide; Glycine; Hematoxylin; Heme; Hemostasis; Immunohistochemistry; Inosine Diphosphate; Male; Necrosis; Neurons; Neuroprotective Agents; Niacinamide; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type III; Picolines; Rats; Rats, Inbred Strains; Reperfusion Injury; Succinates; TNF-Related Apoptosis-Inducing Ligand

2011
Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012, Volume: 17, Issue:5

    Topics: Amino Acid Sequence; Calmodulin; Electron Transport; Flavin Mononucleotide; Heme; Humans; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Mutation; Nitric Oxide Synthase Type II; Protein Isoforms; Sequence Alignment; Spectrometry, Fluorescence

2012
Regulatory role of Glu546 in flavin mononucleotide-heme electron transfer in human inducible nitric oxide synthase.
    Inorganic chemistry, 2013, May-06, Volume: 52, Issue:9

    Topics: Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Heme; Humans; Kinetics; Molecular Docking Simulation; Nitric Oxide Synthase Type II; Oxidation-Reduction; Point Mutation; Protein Conformation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Spectrum Analysis, Raman

2013
Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones.
    Proceedings of the National Academy of Sciences of the United States of America, 2013, May-07, Volume: 110, Issue:19

    Topics: Biofilms; Cytochrome c Group; Cytochromes c; Electrochemistry; Electrodes; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Microscopy, Confocal; Nucleotides; Oxidation-Reduction; Shewanella

2013
Insight into the redox partner interaction mechanism in cytochrome P450BM-3 using molecular dynamics simulations.
    Biopolymers, 2014, Volume: 101, Issue:3

    Topics: Bacterial Proteins; Binding Sites; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Heme; Models, Molecular; Molecular Dynamics Simulation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction

2014
Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation.
    Proceedings of the National Academy of Sciences of the United States of America, 2013, Sep-17, Volume: 110, Issue:38

    Topics: Animals; Calmodulin; Deuterium Exchange Measurement; Dimerization; Electron Transport; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Fluorescence; Heme; Mass Spectrometry; Models, Molecular; Nitric Oxide Synthase Type II; Protein Conformation; Species Specificity

2013
Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant.
    FEBS letters, 2013, Dec-11, Volume: 587, Issue:24

    Topics: Amino Acid Sequence; Animals; Calmodulin; Cytochromes c; Electron Transport; Flavin Mononucleotide; Heme; Isoenzymes; Nitric Oxide; Nitric Oxide Synthase Type I; Protein Binding; Rats

2013
Holoenzyme structures of endothelial nitric oxide synthase - an allosteric role for calmodulin in pivoting the FMN domain for electron transfer.
    Journal of structural biology, 2014, Volume: 188, Issue:1

    Topics: Allosteric Regulation; Animals; Calcium; Calmodulin; Cattle; Electron Transport; Flavin Mononucleotide; Heme; Holoenzymes; Kinetics; Nitric Oxide Synthase Type III; Oxidation-Reduction; Protein Structure, Tertiary

2014
Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics study.
    Journal of inorganic biochemistry, 2015, Volume: 153

    Topics: Calmodulin; Flavin Mononucleotide; Heme; Humans; Iron; Molecular Dynamics Simulation; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Structure, Tertiary

2015
Sequence-Structure-Function Classification of a Catalytically Diverse Oxidoreductase Superfamily in Mycobacteria.
    Journal of molecular biology, 2015, Nov-06, Volume: 427, Issue:22

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Models, Molecular; Molecular Sequence Data; Mycobacterium; Oxidoreductases; Phylogeny; Protein Binding; Sequence Homology, Amino Acid; Substrate Specificity

2015
Elucidating nitric oxide synthase domain interactions by molecular dynamics.
    Protein science : a publication of the Protein Society, 2016, Volume: 25, Issue:2

    Topics: Calmodulin; Electron Transport; Flavin Mononucleotide; Heme; Humans; Molecular Dynamics Simulation; NADP; Nitric Oxide; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Interaction Domains and Motifs

2016
An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.
    Nature, 2016, 11-24, Volume: 539, Issue:7630

    Topics: Binding Sites; Coenzymes; Crystallography, X-Ray; Dimethylamines; Flavin Mononucleotide; Heme; Iron-Sulfur Proteins; Models, Molecular; NADP; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Oxygen; Protein Domains; Protein Subunits; Pseudomonas mendocina; Tetrahydrofolates

2016
A cross-domain charge interaction governs the activity of NO synthase.
    The Journal of biological chemistry, 2018, 03-23, Volume: 293, Issue:12

    Topics: Animals; Catalysis; Cytochromes c; Electron Transport; Electrons; Flavin Mononucleotide; Heme; Kinetics; Models, Molecular; Mutation; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Domains; Rats

2018
Role of an isoform-specific residue at the calmodulin-heme (NO synthase) interface in the FMN - heme electron transfer.
    FEBS letters, 2018, Volume: 592, Issue:14

    Topics: Amino Acid Sequence; Amino Acid Substitution; Calmodulin; Codon, Nonsense; Electron Transport; Flavin Mononucleotide; Heme; Humans; Models, Molecular; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Interaction Domains and Motifs; Protein Isoforms; Protein Structure, Secondary

2018
Cytochrome P450-The Wonderful Nanomachine Revealed through Dynamic Simulations of the Catalytic Cycle.
    Accounts of chemical research, 2019, 02-19, Volume: 52, Issue:2

    Topics: Bacterial Proteins; Camphor 5-Monooxygenase; Catalysis; Catalytic Domain; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Heme; Iron; Models, Chemical; Molecular Dynamics Simulation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen; Protein Binding; Protein Conformation; Quantum Theory; Water

2019
Effect of Macromolecular Crowding on the FMN-Heme Intraprotein Electron Transfer in Inducible NO Synthase.
    Biochemistry, 2019, 07-16, Volume: 58, Issue:28

    Topics: Electron Transport; Ficoll; Flavin Mononucleotide; Heme; Humans; Macromolecular Substances; Nitric Oxide Synthase Type II

2019
Insights on intermolecular FMN-heme domain interaction and the role of linker length in cytochrome P450cin fusion proteins.
    Biological chemistry, 2020, 10-25, Volume: 401, Issue:11

    Topics: Bacterial Proteins; Citrobacter; Cytochrome P-450 Enzyme System; Eucalyptol; Flavin Mononucleotide; Heme; Hydroxylation; Recombinant Fusion Proteins

2020
Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.
    FEBS letters, 2020, Volume: 594, Issue:17

    Topics: Animals; Aspartic Acid; Binding Sites; Cloning, Molecular; Electrons; Escherichia coli; Ficoll; Flavin Mononucleotide; Gene Expression; Genetic Vectors; Heme; HSP90 Heat-Shock Proteins; Humans; Lysine; Molecular Docking Simulation; Mutation; NADP; Nitric Oxide Synthase Type I; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Rats; Recombinant Proteins; Static Electricity

2020
Fluorescence Response and Self-Assembly of a Tweezer-Type Synthetic Receptor Triggered by Complexation with Heme and Its Catabolites.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2021, Apr-12, Volume: 27, Issue:21

    Topics: Flavin Mononucleotide; Fluorescence; Heme; NAD; Receptors, Artificial

2021
An isoform-specific pivot modulates the electron transfer between the flavin mononucleotide and heme centers in inducible nitric oxide synthase.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2020, Volume: 25, Issue:8

    Topics: Electron Transport; Flavin Mononucleotide; Heme; Humans; Isoenzymes; Kinetics; Molecular Docking Simulation; Mutation; Nitric Oxide Synthase Type II; Protein Domains

2020
Heme is responsible for enhanced singlet oxygen deactivation in cytochrome
    Physical chemistry chemical physics : PCCP, 2021, Jul-28, Volume: 23, Issue:29

    Topics: Amino Acid Sequence; Cytochromes c; Flavin Mononucleotide; Heme; Kinetics; Models, Molecular; Oxygen; Photochemistry; Protein Binding; Singlet Oxygen

2021
Interdomain Interactions Modulate the Active Site Dynamics of Human Inducible Nitric Oxide Synthase.
    The journal of physical chemistry. B, 2022, 09-15, Volume: 126, Issue:36

    Topics: Catalytic Domain; Electron Transport; Flavin Mononucleotide; Heme; Heme Oxygenase (Decyclizing); Humans; Ligands; Nitric Oxide; Nitric Oxide Synthase Type II

2022
A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin.
    The Journal of biological chemistry, 2023, Volume: 299, Issue:7

    Topics: Bacterial Proteins; Biological Transport; Flavin Mononucleotide; Flavodoxin; Fusobacterium Infections; Fusobacterium nucleatum; Genes, Bacterial; Heme; Humans; Iron; Oxidation-Reduction; Protein Domains; Tetrapyrroles

2023