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PMID: 6258917 Published · ppublish English Journal Article

The electrochemical proton gradient generated by the fumarate-reductase system in Escherichia coli and its bioenergetic implications.

European journal of biochemistry ·Vol. 113 ·No. 2 ·1981-01-00 ·Pages 369-74

Hellingwerf KJ, Bolscher JG, Konings WN

Abstract

Proton translocation, coupled to electron transfer in the fumarate reductase system, generates and electrochemical potential gradient for protons (delta approximately mu H+). The magnitude of this free energy gradient has been determined in the Escherichia coli strains ML 208-225 and AN 283. The measurements were performed in (inverted) membrane particles, right-side out membrane vesicles and EDTA-treated intact cells in external media of various ionic compositions and pH. The maximal values of delta approximately mu H+ in these three systems were +103, -101 and -105 mV, respectively. This implicates that in E. coli, upon transition from oxygen to fumarate as electron acceptor, the magnitude of the delta approximately mu H+ decreases considerably. This change of delta approximately mu H+ has substantial consequences for the cellular metabolism.

MeSH Terms
Cell Membrane/enzymology Edetic Acid/pharmacology Energy Metabolism Escherichia coli/drug effects,enzymology Hydrogen-Ion Concentration Protons Succinate Dehydrogenase/metabolism
Chemicals
Protons Edetic Acid Succinate Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hellingwerf K J
Bolscher J G
Konings W N
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1981-01-00
Pages
369-74
Language
English
Region
England
NLM ID
0107600
Subset
IM
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