Rotary Movements within the ATP Synthase do not Constitute an Obligatory Element of the Catalytic Mechanism

IUBMB Life

Volumn 55, Issue 8, 2003, Pages 473-481

  Berden, Jan A ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

ATP synthase; Binding change mechanism; Crosslinking; Dual site mechanism; Kinetic analysis; Nucleotide binding sites; Rotary mechanism

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

CATALYSIS; ENERGY CONSERVATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; MOLECULAR MODEL; PROTEIN BINDING; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; REVIEW; ROTATION; STOICHIOMETRY;

ADENOSINE TRIPHOSPHATE; ATP SYNTHETASE COMPLEXES; BINDING SITES; BIOMECHANICS; CATALYSIS; CATALYTIC DOMAIN; CHLOROPLASTS; CROSS-LINKING REAGENTS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; PROTON-TRANSLOCATING ATPASES;

EID: 0142182186     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216540310001612318     Document Type: Review

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