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PMID: 1429541 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Functional sites in F1-ATPases: location and interactions.

Journal of bioenergetics and biomembranes ·Vol. 24 ·No. 5 ·1992-10-00 ·Pages 469-77

Allison WS, Jault JM, Zhuo S, Paik SR

Abstract

This review focuses on the location and interaction of three functional sites in F1-ATPases. These are catalytic sites which are located in beta subunits, noncatalytic nucleotide-binding sites which are located at interfaces of alpha and beta subunits and modulate the hydrolytic activity of the enzyme, and a site that binds inhibitory amphipathic cations which is at an interface of alpha and beta subunits. The latter site may participate in transmission of conformational signals between catalytic sites in F1 and the proton-conducting apparatus of F0 in the intact ATP synthases.

MeSH Terms
Amino Acid Sequence Binding Sites Catalysis Cations/metabolism Molecular Sequence Data Nucleotides/metabolism Proton-Translocating ATPases/chemistry,metabolism Sequence Homology, Amino Acid
Chemicals
Cations Nucleotides Proton-Translocating ATPases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Allison W S
Department of Chemistry, University of California, San Diego, La Jolla 92093-0601.
Jault J M
Zhuo S
Paik S R
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00762364
Published
1992-10-00
Pages
469-77
Language
English
Region
United States
NLM ID
7701859
Subset
IM
Grants
NIGMS NIH HHS · GM16,974 · United States
External Links
PubMed source DOI: 10.1007/BF00762364 View journal details
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