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Solution structures of tetrahaem ferricytochrome c(3) from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity

Solution structures of tetrahaem ferricytochrome c(3) from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity
Solution structures of tetrahaem ferricytochrome c(3) from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity
The NMR structure of the oxidised wild-type cytochrome c(3) from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.
0005-2728
143-153
Messias, A.C.
11074b64-66a9-4298-a25d-bff3ad4427c3
Aguiar, A.P.
2b465210-e4d8-4259-95ad-bb05b28c91c5
Brennan, L.
a178add3-8547-47c8-a03c-17cf2db68a9d
Salgueiro, C.A.
913a1244-243d-4df3-946a-353f2457072b
Saraiva, L.M.
13dfd695-b548-49c1-98ac-3d3c22707f40
Xavier, A.V.
bc590fd4-ed8f-4ad4-a189-b0fc6b63ff2b
Turner, D.L.
bc0db1b4-5aa2-4b89-833e-8f0d31499159
Messias, A.C.
11074b64-66a9-4298-a25d-bff3ad4427c3
Aguiar, A.P.
2b465210-e4d8-4259-95ad-bb05b28c91c5
Brennan, L.
a178add3-8547-47c8-a03c-17cf2db68a9d
Salgueiro, C.A.
913a1244-243d-4df3-946a-353f2457072b
Saraiva, L.M.
13dfd695-b548-49c1-98ac-3d3c22707f40
Xavier, A.V.
bc590fd4-ed8f-4ad4-a189-b0fc6b63ff2b
Turner, D.L.
bc0db1b4-5aa2-4b89-833e-8f0d31499159

Messias, A.C., Aguiar, A.P., Brennan, L., Salgueiro, C.A., Saraiva, L.M., Xavier, A.V. and Turner, D.L. (2006) Solution structures of tetrahaem ferricytochrome c(3) from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1757 (2), 143-153. (doi:10.1016/j.bbabio.2006.01.007).

Record type: Article

Abstract

The NMR structure of the oxidised wild-type cytochrome c(3) from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.

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Published date: 2006

Identifiers

Local EPrints ID: 44497
URI: http://eprints.soton.ac.uk/id/eprint/44497
ISSN: 0005-2728
PURE UUID: d8b756d7-7a73-4519-85e3-a3a3ad061583

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Date deposited: 07 Mar 2007
Last modified: 15 Mar 2024 09:04

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Contributors

Author: A.C. Messias
Author: A.P. Aguiar
Author: L. Brennan
Author: C.A. Salgueiro
Author: L.M. Saraiva
Author: A.V. Xavier
Author: D.L. Turner

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