The University of Southampton
University of Southampton Institutional Repository

NMR redox studies of flavocytochrome c(3) from Shewanella frigidimarina

NMR redox studies of flavocytochrome c(3) from Shewanella frigidimarina
NMR redox studies of flavocytochrome c(3) from Shewanella frigidimarina
Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages.
shewanella, electron tranfer protein, multihaem, flavocytochrome, nmr, paramagnetic shiftsfumarate reductase, cytochrome c(3), desulfovibrio-vulgaris, energytransduction, putrefaciens mr-1, electron-transfer, heme core, cooperativity, respiration, ncimb400
0020-1693
379-381
Pessanha, M.
4314f0ea-71a6-49f0-b68d-0f3ae8a74fba
Turner, D. L.
158980fd-3487-480b-baba-15102dfb64b4
Rothery, E. L.
f6a59997-8e13-4c10-bcfc-340c08fc53e5
Pankhurst, K. L.
3d9eb18b-69ee-4088-a760-b007912b3723
Reid, G. A.
1120e44f-b6db-4b84-bcf8-c58a20df7585
Chapman, S. K.
69bd0a6b-3dc1-44e5-97e4-bca3808c52e9
Xavier, A. V.
b73ea5e9-4b82-441a-96e8-7907c5fab76b
Salgueiro, C. A.
f2558f8c-9e4d-4f20-8c36-9a77e86e23c7
Pessanha, M.
4314f0ea-71a6-49f0-b68d-0f3ae8a74fba
Turner, D. L.
158980fd-3487-480b-baba-15102dfb64b4
Rothery, E. L.
f6a59997-8e13-4c10-bcfc-340c08fc53e5
Pankhurst, K. L.
3d9eb18b-69ee-4088-a760-b007912b3723
Reid, G. A.
1120e44f-b6db-4b84-bcf8-c58a20df7585
Chapman, S. K.
69bd0a6b-3dc1-44e5-97e4-bca3808c52e9
Xavier, A. V.
b73ea5e9-4b82-441a-96e8-7907c5fab76b
Salgueiro, C. A.
f2558f8c-9e4d-4f20-8c36-9a77e86e23c7

Pessanha, M., Turner, D. L., Rothery, E. L., Pankhurst, K. L., Reid, G. A., Chapman, S. K., Xavier, A. V. and Salgueiro, C. A. (2003) NMR redox studies of flavocytochrome c(3) from Shewanella frigidimarina. Inorganica Chimica Acta, 356, 379-381. (doi:10.1016/S0020-1693(03)00179-8).

Record type: Article

Abstract

Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages.

This record has no associated files available for download.

More information

Published date: 3 December 2003
Keywords: shewanella, electron tranfer protein, multihaem, flavocytochrome, nmr, paramagnetic shiftsfumarate reductase, cytochrome c(3), desulfovibrio-vulgaris, energytransduction, putrefaciens mr-1, electron-transfer, heme core, cooperativity, respiration, ncimb400

Identifiers

Local EPrints ID: 20064
URI: http://eprints.soton.ac.uk/id/eprint/20064
ISSN: 0020-1693
PURE UUID: 09fe34a1-d9c9-4a2d-ad80-f2b2ffb5cab5

Catalogue record

Date deposited: 23 Feb 2006
Last modified: 15 Mar 2024 06:21

Export record

Altmetrics

Contributors

Author: M. Pessanha
Author: D. L. Turner
Author: E. L. Rothery
Author: K. L. Pankhurst
Author: G. A. Reid
Author: S. K. Chapman
Author: A. V. Xavier
Author: C. A. Salgueiro

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.

×