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Volumn 1698, Issue 2, 2004, Pages 197-202

Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor

Author keywords

ATP hydrolysis; Binding cooperativity; Chemomechanics; F1 ATPase; Molecular motor

Indexed keywords

ADENOSINE TRIPHOSPHATE; HYDROLASE; MOLECULAR MOTOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 2342453196     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.11.033     Document Type: Article
Times cited : (11)

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    • note
    • 1-ATPase, ATP hydrolysis and reversible synthesis are at fast equilibrium. O18 exchange studies confirmed that ATP and ADP.Pi interconvert rapidly in the active site [1, 13]. To date the number of nucleotides and, in particular, the conformations bounded with ATP or ADP.Pi are not dynamically distinguishable [14, 34], unless Pi or ADP is further released from the active site.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.