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PMID: 3650 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

ATP synthesis driven by a protonmotive force in Streptococcus lactis.

The Journal of membrane biology ·Vol. 25 ·No. 3-4 ·1975-00-00 ·Pages 285-310

Maloney PC, Wilson TH

Abstract

An electrochemical potential difference for hydrogen ions ( a protonmotive force) was artifically imposed across the membrane of the anaerobic bacterium Streptococcus lactis. When cells were exposed to the ionophore, valinomycin, the electrical gradient was established by a potassium diffusion potential. A chemical gradient of protons was established by manipulating the transmembrane pH gradient. When the protonmotive force attained a value of 215 mV or greater, net ATP synthesis was catalyzed by the membrane-bound Ca++, Mg++ -stimulated ATPase. This was true whether the protonmotive force was dominated by the membrane potential (negative inside) or the pH gradient (alkaline inside). Under these conditions, ATP synthesis could be blocked by the ATPase inhibitor, dicyclohexylcarbodiimide, or by ionophores which rendered the membrane specifically permeable to protons. These observations provide strong evidence in support of the chemiosmotic hypothesis, which states that the membrane-bound ATPase couples the inward movement of protons to the synthesis of ATP.

MeSH Terms
Adenosine Diphosphate/metabolism Adenosine Triphosphatases/metabolism Adenosine Triphosphate/biosynthesis Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone/pharmacology Hydrogen/metabolism Hydrogen-Ion Concentration Lactococcus lactis/metabolism Membrane Potentials Potassium/metabolism Valinomycin/pharmacology
Chemicals
Valinomycin Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone Adenosine Diphosphate Hydrogen Adenosine Triphosphate Adenosine Triphosphatases Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Maloney P C
Wilson T H
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Article Info
Journal
The Journal of membrane biology
Abbr.
J Membr Biol
ISSN
0022-2631
DOI
10.1007/BF01868580
Published
1975-00-00
Pages
285-310
Language
English
Region
United States
NLM ID
0211301
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01868580 View journal details
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