The University of Southampton
University of Southampton Institutional Repository

Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate

Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate
Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate
Glutamate induced the synthesis of 2-oxoglutarate dehydrogenase 50-fold during anaerobic growth of Citrobacter freundii and, in the absence of glutamate, this enzyme was even more active in cultures sparged with N2/CO2 (95:5, v/v). Enzyme synthesis was partially repressed when the inlet gas was passed through heated copper but totally repressed when the inlet gas was passed through alkaline pyrogallol and reduced benzyl viologen (a treatment which would remove CO2 as well as O2). Fumarate hydratase activity also decreased but alcohol dehydrogenase and the sum of the succinate dehydrogenase and fumarate reductase activities increased when residual O2 was removed from the sparging gas. Soluble cytochromes a 1 and c 552.5 were detected in rigorously anaerobic cultures. Thus traces of O2 which contaminate commercial compressed N2 are sufficient to induce 2-oxoglutarate dehydrogenase synthesis and to affect significantly the synthesis and incorporation of respiratory chain components into the cytoplasmic membrane.
0022-1287
355-359
Keevil, C.W.
cb7de0a7-ce33-4cfa-af52-07f99e5650eb
Hough, J.S.
a603598e-ec1d-44fa-863c-ccc138b36704
Cole, J.A.
1b68cada-8d91-4bfc-8d66-df505e309160
Keevil, C.W.
cb7de0a7-ce33-4cfa-af52-07f99e5650eb
Hough, J.S.
a603598e-ec1d-44fa-863c-ccc138b36704
Cole, J.A.
1b68cada-8d91-4bfc-8d66-df505e309160

Keevil, C.W., Hough, J.S. and Cole, J.A. (1979) Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate. Journal of General Microbiology, 114 (2), 355-359. (doi:10.1099/00221287-114-2-355).

Record type: Article

Abstract

Glutamate induced the synthesis of 2-oxoglutarate dehydrogenase 50-fold during anaerobic growth of Citrobacter freundii and, in the absence of glutamate, this enzyme was even more active in cultures sparged with N2/CO2 (95:5, v/v). Enzyme synthesis was partially repressed when the inlet gas was passed through heated copper but totally repressed when the inlet gas was passed through alkaline pyrogallol and reduced benzyl viologen (a treatment which would remove CO2 as well as O2). Fumarate hydratase activity also decreased but alcohol dehydrogenase and the sum of the succinate dehydrogenase and fumarate reductase activities increased when residual O2 was removed from the sparging gas. Soluble cytochromes a 1 and c 552.5 were detected in rigorously anaerobic cultures. Thus traces of O2 which contaminate commercial compressed N2 are sufficient to induce 2-oxoglutarate dehydrogenase synthesis and to affect significantly the synthesis and incorporation of respiratory chain components into the cytoplasmic membrane.

Full text not available from this repository.

More information

Published date: 1 October 1979

Identifiers

Local EPrints ID: 437346
URI: http://eprints.soton.ac.uk/id/eprint/437346
ISSN: 0022-1287
PURE UUID: 0c014bc6-da08-4310-a4a4-b24d565799e2
ORCID for C.W. Keevil: ORCID iD orcid.org/0000-0003-1917-7706

Catalogue record

Date deposited: 24 Jan 2020 17:31
Last modified: 16 Mar 2021 02:37

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×