The Escherichia coli F(O)F1 γM23K uncoupling mutant has a higher K0.5 for P(i). Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway

Biochemistry

Volumn 36, Issue 42, 1997, Pages 12961-12969

  Al Shawi, Marwan K ^a   Ketchum, Christian J ^a   Nakamoto, Robert K ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; ADENOSINE DIPHOSPHATE; PHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONFORMATIONAL TRANSITION; DISSOCIATION CONSTANT; ENZYME BINDING; ENZYME KINETICS; ENZYME SYNTHESIS; ESCHERICHIA COLI; HYDROGEN BOND; HYDROLYSIS; MUTATION; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL; THERMODYNAMICS; BINDING SITE; CELL MEMBRANE; CHEMICAL MODEL; CHEMISTRY; ENZYMOLOGY; KINETICS; METABOLISM; POINT MUTATION; PROTEIN CONFORMATION;

ADENOSINE DIPHOSPHATE; BINDING SITES; CELL MEMBRANE; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; MODELS, CHEMICAL; PHOSPHATES; POINT MUTATION; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; THERMODYNAMICS;

EID: 0030612021     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971478r     Document Type: Article

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