The University of Southampton
University of Southampton Institutional Repository

Functional properties of type I and type II cytochromes c(3) from Desulfovibrio africanus

Functional properties of type I and type II cytochromes c(3) from Desulfovibrio africanus
Functional properties of type I and type II cytochromes c(3) from Desulfovibrio africanus
Type I cytochrome c3 is a key protein in the bioenergetic metabolism of Desulfovibrio spp., mediating electron transfer between periplasmic hydrogenase and multihaem cytochromes associated with membrane bound complexes, such as type II cytochrome c3. This work presents the NMR assignment of the haem substituents in type I cytochrome c3 isolated from Desulfovibrio africanus and the thermodynamic and kinetic characterisation of type I and type II cytochromes c3 belonging to the same organism. It is shown that the redox properties of the two proteins allow electrons to be transferred between them in the physiologically relevant direction with the release of energised protons close to the membrane where they can be used by the ATP synthase.
sulfate-reducing bacteria, electron transfer rates, axial ligand orientation, nife, hydrogenase, thermodynamic characterisation, electron-transfer proteins, hildenborough, energy transduction, desulfovibrio africanus, multicentre protein, cytochrome c3, tetraheme cytochromes, hmc operon, proton thruster, desulfuricans atcc 27774, subsp vulgaris
0005-2728
178-188
Paquete, C.M.
33d20dad-2d71-4a8d-bc17-7e351e4d080d
Pereira, P.M.
456a96f5-10bd-4448-b25f-b78cfde3265a
Catarino, T.
02e16379-0fda-4ecd-828c-e10bb0e36502
Turner, D.L.
bc0db1b4-5aa2-4b89-833e-8f0d31499159
Louro, R.O.
5473a453-e54d-4559-968b-abfdc1f36d67
Xavier, A.V.
bc590fd4-ed8f-4ad4-a189-b0fc6b63ff2b
Paquete, C.M.
33d20dad-2d71-4a8d-bc17-7e351e4d080d
Pereira, P.M.
456a96f5-10bd-4448-b25f-b78cfde3265a
Catarino, T.
02e16379-0fda-4ecd-828c-e10bb0e36502
Turner, D.L.
bc0db1b4-5aa2-4b89-833e-8f0d31499159
Louro, R.O.
5473a453-e54d-4559-968b-abfdc1f36d67
Xavier, A.V.
bc590fd4-ed8f-4ad4-a189-b0fc6b63ff2b

Paquete, C.M., Pereira, P.M., Catarino, T., Turner, D.L., Louro, R.O. and Xavier, A.V. (2007) Functional properties of type I and type II cytochromes c(3) from Desulfovibrio africanus. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1767 (2), 178-188. (doi:10.1016/j.bbabio.2007.01.012).

Record type: Article

Abstract

Type I cytochrome c3 is a key protein in the bioenergetic metabolism of Desulfovibrio spp., mediating electron transfer between periplasmic hydrogenase and multihaem cytochromes associated with membrane bound complexes, such as type II cytochrome c3. This work presents the NMR assignment of the haem substituents in type I cytochrome c3 isolated from Desulfovibrio africanus and the thermodynamic and kinetic characterisation of type I and type II cytochromes c3 belonging to the same organism. It is shown that the redox properties of the two proteins allow electrons to be transferred between them in the physiologically relevant direction with the release of energised protons close to the membrane where they can be used by the ATP synthase.

This record has no associated files available for download.

More information

Published date: 2007
Keywords: sulfate-reducing bacteria, electron transfer rates, axial ligand orientation, nife, hydrogenase, thermodynamic characterisation, electron-transfer proteins, hildenborough, energy transduction, desulfovibrio africanus, multicentre protein, cytochrome c3, tetraheme cytochromes, hmc operon, proton thruster, desulfuricans atcc 27774, subsp vulgaris

Identifiers

Local EPrints ID: 54355
URI: http://eprints.soton.ac.uk/id/eprint/54355
ISSN: 0005-2728
PURE UUID: 85b5457b-b0f2-4eee-bb8b-4a1aed14d4f4

Catalogue record

Date deposited: 31 Jul 2008
Last modified: 15 Mar 2024 10:47

Export record

Altmetrics

Contributors

Author: C.M. Paquete
Author: P.M. Pereira
Author: T. Catarino
Author: D.L. Turner
Author: R.O. Louro
Author: A.V. Xavier

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.

×