Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of γ-β subunit interactions in the catalytic dwell

Journal of Biological Chemistry

Volumn 284, Issue 33, 2009, Pages 22401-22410

  Sekiya, Mizuki ^a   Nakamoto, Robert K ^b   Al Shawi, Marwan K ^b   Nakanishi Matsui, Mayumi ^a   Futai, Masamitsu ^a  

^a IWATE MEDICAL UNIVERSITY   (Japan)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARRHENIUS; ATP SYNTHASE; CATALYTIC CYCLES; ELASTIC ENERGY; ENERGY PATHWAY; ROTATION RATE; ROTOR-STATOR INTERACTIONS; SINGLE MOLECULE; TEMPERATURE DEPENDENCE; TEMPERATURE DEPENDENT; VISCOUS DRAG; WILD TYPES;

ENZYMES; ESCHERICHIA COLI; ROTATION; STATORS;

ACTIVATION ENERGY;

ASPARTIC ACID; GLUTAMIC ACID; LYSINE; METHIONINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENERGY CONSUMPTION; ENZYME KINETICS; ENZYME SUBUNIT; ESCHERICHIA COLI; MUTANT; PRIORITY JOURNAL; PROTEIN INTERACTION; TEMPERATURE DEPENDENCE; WILD TYPE;

ADENOSINE TRIPHOSPHATE; CATALYSIS; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; LYSINE; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MUTATION; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; TEMPERATURE; THERMODYNAMICS; TIME FACTORS;

ESCHERICHIA COLI;

EID: 69249148218     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.009019     Document Type: Article

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