Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1

Journal of Bioenergetics and Biomembranes

Volumn 28, Issue 5, 1996, Pages 403-408

  Cross, Richard L ^a   Duncan, Thomas M ^a  

^a SUNY UPSTATE MEDICAL UNIVERSITY   (United States)

Author keywords

Binding change mechanism; F0F1 ATP synthase; oxidative phosphorylation; rotary mechanism; subunit rotation

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBUNIT; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PROTEIN CROSS LINKING; PROTON TRANSPORT; REVIEW; BINDING SITE; CHEMISTRY; ENERGY METABOLISM; METABOLISM; PROTEIN CONFORMATION; TRANSPORT AT THE CELLULAR LEVEL;

BINDING SITES; BIOLOGICAL TRANSPORT; ENERGY METABOLISM; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; PROTONS;

EID: 0029658151     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02113981     Document Type: Review

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