Does the γ subunit move to an abortive position for ATP hydrolysis when the F1·ADP·Mg complex isomerizes to the inactive F1·ADP·Mg complex?

Journal of Bioenergetics and Biomembranes

Volumn 28, Issue 5, 1996, Pages 433-438

  Allison, William S ^a   Jault, Jean Michael ^b   Dou, Chao ^a   Grodsky, Neil B ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b INSTITUT DE BIOLOGIE ET CHIMIE DES PROTÉINES   (France)

Author keywords

ADP complex; F1; F1 atpases; F1 mg ; Subcomplex; 3 1 subcomplex; 3 3 ; 3 3

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MAGNESIUM;

BINDING AFFINITY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HYDROLYSIS; PHOSPHATE METABOLISM; REVIEW;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; CA(2+) MG(2+)-ATPASE; CATALYSIS; HYDROLYSIS; PROTON-TRANSLOCATING ATPASES; STEREOISOMERISM;

EID: 0029852943     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02113985     Document Type: Article

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