Escherichia coli ATP synthase (F-ATPase)

catalytic site and regulation of H+ translocation.

M. Futai, A. Iwamoto, Hiroshi Omote, Y. Orita, K. Shin, R. K. Nakamoto, M. Maeda

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

We discuss our recent results on the Escherichia coli F-ATPase, in particular its catalytic site in the beta subunit and regulation of H+ transport by the gamma subunit. Affinity labelling experiments suggest that beta Lys-155 in the glycine-rich sequence is near the gamma-phosphate moiety of ATP bound at the catalytic site. The enzyme loses activity upon introduction of missense mutations in beta Lys-155 or beta Thr-156 and changes catalytic properties upon introduction of other mutations. By analysis of mutations and their pseudo revertants, residues beta Ser-174, beta Glu-192 and beta Val-198 were found to be located near the glycine-rich sequence. The combined approaches of chemical labelling and genetics have been fruitful in visualizing the structure of the catalytic site. Analysis of mutations in the gamma subunit suggests that this subunit has an essential role in coupling catalysis with proton translocation.

Original languageEnglish
Pages (from-to)443-449
Number of pages7
JournalJournal of Experimental Biology
Volume172
Publication statusPublished - Nov 1992
Externally publishedYes

Fingerprint

H-transporting ATP synthase
active sites
translocation
adenosinetriphosphatase
Adenosine Triphosphatases
mutation
Catalytic Domain
Adenosine Triphosphate
Escherichia coli
Glycine
Mutation
missense mutation
Missense Mutation
Catalysis
catalytic activity
protons
Protons
catalysis
Phosphates
phosphates

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

Cite this

Futai, M., Iwamoto, A., Omote, H., Orita, Y., Shin, K., Nakamoto, R. K., & Maeda, M. (1992). Escherichia coli ATP synthase (F-ATPase): catalytic site and regulation of H+ translocation. Journal of Experimental Biology, 172, 443-449.

Escherichia coli ATP synthase (F-ATPase) : catalytic site and regulation of H+ translocation. / Futai, M.; Iwamoto, A.; Omote, Hiroshi; Orita, Y.; Shin, K.; Nakamoto, R. K.; Maeda, M.

In: Journal of Experimental Biology, Vol. 172, 11.1992, p. 443-449.

Research output: Contribution to journalArticle

Futai, M, Iwamoto, A, Omote, H, Orita, Y, Shin, K, Nakamoto, RK & Maeda, M 1992, 'Escherichia coli ATP synthase (F-ATPase): catalytic site and regulation of H+ translocation.', Journal of Experimental Biology, vol. 172, pp. 443-449.
Futai, M. ; Iwamoto, A. ; Omote, Hiroshi ; Orita, Y. ; Shin, K. ; Nakamoto, R. K. ; Maeda, M. / Escherichia coli ATP synthase (F-ATPase) : catalytic site and regulation of H+ translocation. In: Journal of Experimental Biology. 1992 ; Vol. 172. pp. 443-449.
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