Regulation of the F0F1-ATP synthase: The conformation of subunit ε might be determined by directionality of subunit γ rotation

FEBS Letters

Volumn 579, Issue 23, 2005, Pages 5114-5118

  Feniouk, Boris A ^a,b   Junge, Wolfgang ^a  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Activation; ADP inhibition; ATP synthase; Protonmotive force; Regulation; Subunit

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; F0F1 PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; ENZYME REGULATION; HYDROLYSIS; HYPOTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON MOTIVE FORCE; PROTON TRANSPORT; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; REVIEW;

ADENOSINE DIPHOSPHATE; ANIMALS; BACTERIAL PROTEINS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTON-TRANSLOCATING ATPASES;

EID: 24944464164     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.08.030     Document Type: Article

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