Effect of the insertion of a glycine residue into the loop spanning residues 536-541 on the semiquinone state and redox properties of the flavin mononucleotide-binding domain of flavocytochrome p450bm-3 from bacillus megaterium

Biochemistry

Volumn 47, Issue 52, 2008, Pages 13788-13799

  Chen, Huai Chun ^b   Swenson, Richard P ^a,b  

^a Department of Biochemistry ^*  (United States)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE GROUPS; BACILLUS MEGATERIUM; BACKBONE CARBONYL; BINDING DOMAIN; BINDING LOOP; COFACTORS; CONFORMATIONAL CHANGE; CYTOCHROME C; ELECTRON TRANSFERRING; FLAVIN MONONUCLEOTIDES; FLAVOCYTOCHROME; FLAVODOXIN; GLYCINE RESIDUES; HYDROGEN BONDINGS; MIDPOINT POTENTIALS; MOLECULAR MODELS; NADPH-CYTOCHROME P450 REDUCTASE; NH GROUPS; NITRIC-OXIDE SYNTHASE; NMR DATA; OXIDIZED STATE; PURIFIED PROTEIN; RAPID REDUCTION; REDOX PROPERTY; REDUCTASE ACTIVITY; SEMIQUINONES; STRUCTURAL CHARACTERISTICS; STRUCTURAL SIMILARITY; THERMODYNAMIC STABILIZATION; WILD TYPES;

AMIDES; BACTERIOLOGY; ENZYME ACTIVITY; HYDROGEN; NITRIC OXIDE; PROTEINS;

HYDROGEN BONDS;

ASPARAGINE; CARBONYL DERIVATIVE; CYTOCHROME B5 REDUCTASE; CYTOCHROME P450; CYTOCHROME P450 REDUCTASE; DIFLAVIN REDUCTASE; FLAVINE MONONUCLEOTIDE; FLAVOCYTOCHROME P450BM3; FLAVODOXIN; GLYCINE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SEMIQUINONE; TYROSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; FLAVIN MONONUCLEOTIDE SEMIQUINONE; FLAVOCYTOCHROME P450 BM3 MONOXYGENASES; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

ARTICLE; ATOM; BACILLUS MEGATERIUM; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR MODEL; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PURIFICATION; PROTEIN STRUCTURE; STOICHIOMETRY; WILD TYPE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COENZYME; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION;

BACILLUS MEGATERIUM;

BACILLUS MEGATERIUM; BACTERIAL PROTEINS; BINDING SITES; COENZYMES; CYTOCHROME P-450 ENZYME SYSTEM; FLAVIN MONONUCLEOTIDE; GLYCINE; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTAGENESIS, INSERTIONAL; NADPH-FERRIHEMOPROTEIN REDUCTASE; OXIDATION-REDUCTION; PROTEIN CONFORMATION;

EID: 58849120066     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi800954h     Document Type: Article

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