Novel insights into the chemical mechanism of ATP synthase. Evidence that in the transition state the γ-phosphate of ATP is near the conserved alanine within the P-loop of the β-subunit

Journal of Biological Chemistry

Volumn 272, Issue 30, 1997, Pages 18875-18881

  Ko, Young Hee ^a   Bianchet, Mario ^a   Amzel, L Mario ^a   Pedersen, Peter L ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; ALANINE; MAGNESIUM ION; MYOSIN; NUCLEOTIDE BINDING PROTEIN; ORTHOVANADIC ACID; PHOSPHATE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SUBUNIT; PRIORITY JOURNAL;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID SEQUENCE; ANIMALS; BOROHYDRIDES; CONSERVED SEQUENCE; HYDROLYSIS; KINETICS; MAGNESIUM CHLORIDE; MALE; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PHOSPHORIC ACID ESTERS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTON-TRANSLOCATING ATPASES; RATS; RATS, SPRAGUE-DAWLEY; ULTRAVIOLET RAYS; VANADATES;

EID: 0001694870     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.30.18875     Document Type: Article

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