Inhibitory Mg-ADP-fluoroaluminate complexes bound to catalytic sites of F(1)-ATPases: are they ground-state or transition-state analogs?

Autor:	W S, Allison, H, Ren, C, Dou
Rok vydání:	2004
Předmět:	Adenosine Diphosphate Models Molecular Kinetics Protein Subunits Proton-Translocating ATPases Catalytic Domain Mutagenesis Site-Directed Fluorine Models Biological Aluminum
Zdroj:	Journal of bioenergetics and biomembranes. 32(5)
ISSN:	1573-6881
Popis:	Schemes are proposed for coupling sequential opening and closing the three catalytic sites of F(1) to rotation of the gamma subunit during ATP synthesis and hydrolysis catalyzed by the F(o)F(1)-ATP synthase. A prominent feature of the proposed mechanisms is that the transition state during ATP synthesis is formed when a catalytic site is in the process of closing and that the transition state during ATP hydrolysis is formed when a catalytic site is in the process of opening. The unusual kinetics of formation of Mg-ADP-fluoroaluminate complexes in one or two catalytic sites of nucleotide-depleted MF(1) and wild-type and mutant alpha(3)beta(3)gamma subcomplexes of TF(1) are also reviewed. From these considerations, it is concluded that Mg-ADP-fluoroaluminate complexes formed at catalytic sites of isolated F(1)-ATPases or F(1) in membrane-bound F(o)F(1) are ground-state analogs.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::f095913a266ffd6fc0bf1902c212edc2 https://pubmed.ncbi.nlm.nih.gov/15254389 Zobrazit plný text záznamu Full text from SpringerLink