Functional characterization of the re-face loop spanning residues 536-541 and its interactions with the cofactor in the flavin mononucleotide-binding domain of flavocytochrome p450 from Bacillus megaterium

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5131-5141

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

^a OHIO STATE UNIVERSITY   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS MEGATERIUM; BINDING DOMAIN; COFACTOR; CYTOCHROME P450 REDUCTASE; ELECTRON DONORS; ELECTRON TRANSFER MECHANISMS; FLAVIN MONONUCLEOTIDE; FLAVOCYTOCHROME; FLAVODOXIN; FUNCTIONAL CHARACTERIZATION; H-BONDING INTERACTION; HEME IRON; IONIZATION STATE; LOOP REGIONS; MIDPOINT POTENTIALS; MONOOXYGENASE; NUCLEAR MAGNETIC RESONANCE STUDIES; REDOX PROPERTY; REDOX STATE; SEMIQUINONE; STRUCTURAL HOMOLOGY; THERMODYNAMICALLY STABLE;

AMIDES; AMINO ACIDS; BACTERIOLOGY; ELECTRON TRANSITIONS; HYDROGEN; HYDROGEN BONDS; KETONES; MAGNETIC RESONANCE; MAMMALS; NUCLEAR MAGNETIC RESONANCE; PHENOLS; PORPHYRINS;

MAGNETIC DOMAINS;

ALANINE; ARGININE; ASPARAGINE; BACTERIAL ENZYME; FLAVINE MONONUCLEOTIDE; FLAVOCYTOCHROME P450; GLYCINE; HISTIDINE; PROLINE; SEMIQUINONE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS MEGATERIUM; CONTROLLED STUDY; HYDROGEN BOND; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; BACILLUS MEGATERIUM; BACTERIAL PROTEINS; BINDING SITES; CYTOCHROME P-450 ENZYME SYSTEM; FLAVIN MONONUCLEOTIDE; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NADPH-FERRIHEMOPROTEIN REDUCTASE; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

BACILLUS MEGATERIUM; BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 67049087902     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900607q     Document Type: Article

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