The reconstitution of functional respiratory chains in membranes from electron-transport-deficient mutants of Escherichia coli as demonstrated by quenching of atebrin fluorescence.

The Biochemical journal ·Vol. 142 ·No. 3 ·1974-09-00 ·Pages 703-6

Haddock BA, Downie JA

Abstract

Measurements were made of electron-transport-dependent quenching of atebrin fluorescence in particles prepared from mutants of Escherichia coli unable to synthesize either ubiquinone or haem. Such quenching was either absent (in haem-deficient particles) or decreased (in ubiquinone-deficient particles), but was restored under conditions used to reconstitute oxidase activities. It is concluded that the reconstitution of oxidase activity, in both cases, is associated with the formation of a functional, proton-translocating, respiratory chain.

MeSH Terms

Cell Membrane/drug effects,metabolism Cyanides/pharmacology Electron Transport Escherichia coli/drug effects,metabolism Fluorescent Dyes Mutation NAD/metabolism Oxidation-Reduction Quinacrine Spectrometry, Fluorescence

Chemicals

Cyanides Fluorescent Dyes NAD Quinacrine

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Haddock B A

Downie J A

References (16)

16 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1420703

Published

1974-09-00

Pages

703-6

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1168339

Subset

External Links

PubMed source DOI: 10.1042/bj1420703 PMC Full Text View journal details

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The reconstitution of functional respiratory chains in membranes from electron-transport-deficient mutants of Escherichia coli as demonstrated by quenching of atebrin fluorescence.

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