A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin

Biochemistry

Volumn 46, Issue 39, 2007, Pages 11137-11146

  Ma, John K ^a   Wang, Yongting ^a,c   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)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; ENZYME ACTIVITY; GENE EXPRESSION; PROTON TRANSFER;

AMICYANIN; ELECTRON ACCEPTORS; ELECTRON TRANSFER; ELECTRONIC COUPLINGS; METHYLAMINE DEHYDROGENASE; MUTATIONS;

PROTEINS;

ALANINE; AMICYANIN; AMINE DEHYDROGENASE; AMINO ACID; GLYCINE; LEUCINE; LYSINE; METHIONINE; PROLINE; PROTON;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; ELECTRON TRANSPORT; ENERGY; PARAMETER; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON TRANSPORT; SEQUENCE ANALYSIS;

AMINO ACIDS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT; HYDROPHOBICITY; KINETICS; METHIONINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PARACOCCUS DENITRIFICANS; TEMPERATURE;

EID: 34848922789     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7012307     Document Type: Article

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