Chemical modification of the beta-subunit isolated from a membrane-bound Fo-F1-ATP synthase: modification by 4-chloro-7-nitrobenzofurazan does not inhibit restoration of ATP synthesis or hydrolysis.

Biochemical and biophysical research communications ·Vol. 108 ·No. 2 ·1982-09-30 ·Pages 881-7

Khananshvili D, Gromet-Elhanan Z

Abstract

暂无摘要

MeSH Terms

4-Chloro-7-nitrobenzofurazan Adenosine Triphosphatases/metabolism Binding Sites Dicyclohexylcarbodiimide Protein Conformation Proton-Translocating ATPases Rhodospirillum rubrum/enzymology Structure-Activity Relationship

Chemicals

Dicyclohexylcarbodiimide Adenosine Triphosphatases Proton-Translocating ATPases 4-Chloro-7-nitrobenzofurazan

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Khananshvili D

Gromet-Elhanan Z

Article Info

Journal

Biochemical and biophysical research communications

Abbr.

Biochem Biophys Res Commun

ISSN

0006-291X

DOI

10.1016/0006-291x(82)90913-5

Published

1982-09-30

Pages

881-7

Language

English

Region

United States

NLM ID

0372516

Subset

External Links

PubMed source DOI: 10.1016/0006-291x(82)90913-5 View journal details

Analysis Services

Chemical modification of the beta-subunit isolated from a membrane-bound Fo-F1-ATP synthase: modification by 4-chloro-7-nitrobenzofurazan does not inhibit restoration of ATP synthesis or hydrolysis.

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