Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated

Biochemistry

Volumn 45, Issue 27, 2006, Pages 8284-8293

  Ma, John K ^a   Carrell, Christopher J ^b   Mathews, F Scott ^b   Davidson, Victor L ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; COPPER; CRYSTAL STRUCTURE; ELECTRON TRANSITIONS; GLYCEROL; MATHEMATICAL MODELS; MUTAGENESIS; PARAMETER ESTIMATION; PROTEINS; SPECTROSCOPIC ANALYSIS;

HYDROPHOBIC INTERACTIONS; METHYLAMINE DEHYDROGENASE (MADH); RATE OF ELECTRON TRANSFER (ET); TRYPTOPHAN TRYPTOPHYLQUINONE (TTQ);

ENZYMES;

AMICYANIN; AMINE DEHYDROGENASE; AZURIN; BENZOQUINONE; COPPER PROTEIN; CYTOCHROME C; GLYCINE; HYDROQUINONE; O QUINOL TRYPTOPHAN TRYPTOPHYLQUINONE; PROLINE; QUINONE DERIVATIVE; SEMIQUINONE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; HYDROPHOBICITY; OXIDATION REDUCTION POTENTIAL; PARACOCCUS DENITRIFICANS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE; X RAY DIFFRACTION;

AMINO ACID SUBSTITUTION; AZURIN; BACTERIAL PROTEINS; BINDING SITES; CARRIER PROTEINS; CRYSTALLOGRAPHY; ELECTRON TRANSPORT; GLYCINE; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PARACOCCUS DENITRIFICANS; PROLINE; PROTEIN CONFORMATION; SPECTRUM ANALYSIS;

EID: 33745847159     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0605134     Document Type: Article

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