Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity

Ana C. Messias; António P. Aguiar; Lorraine Brennan; Carlos A. Salgueiro; Lígia M. Saraiva; António V. Xavier; David L. Turner

doi:10.1016/j.bbabio.2006.01.007

Solution structures of tetrahaem ferricytochrome c₃ from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity

Ana C. Messias, António P. Aguiar, Lorraine Brennan, Carlos A. Salgueiro, Lígia M. Saraiva, António V. Xavier, David L. Turner

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

The NMR structure of the oxidised wild-type cytochrome c₃ 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.

Original language	English
Pages (from-to)	143-153
Number of pages	11
Journal	Biochimica et Biophysica Acta-Bioenergetics
Volume	1757
Issue number	2
DOIs	https://doi.org/10.1016/j.bbabio.2006.01.007
Publication status	Published - Feb 2006

Keywords

Cytochrome c
Multihaem cytochromes
NMR
Redox proteins
Tetrahaem cytochrome c

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10.1016/j.bbabio.2006.01.007

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Messias, A. C., Aguiar, A. P., Brennan, L., Salgueiro, C. A., Saraiva, L. M., Xavier, A. V., & Turner, D. L. (2006). Solution structures of tetrahaem ferricytochrome c₃ from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity. Biochimica et Biophysica Acta-Bioenergetics, 1757(2), 143-153. https://doi.org/10.1016/j.bbabio.2006.01.007

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title = "Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity",

abstract = "The NMR structure of the oxidised wild-type cytochrome c3 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.",

keywords = "Cytochrome c, Multihaem cytochromes, NMR, Redox proteins, Tetrahaem cytochrome c",

author = "Messias, {Ana C.} and Aguiar, {Ant{\'o}nio P.} and Lorraine Brennan and Salgueiro, {Carlos A.} and Saraiva, {L{\'i}gia M.} and Xavier, {Ant{\'o}nio V.} and Turner, {David L.}",

year = "2006",

month = feb,

doi = "10.1016/j.bbabio.2006.01.007",

language = "English",

volume = "1757",

pages = "143--153",

journal = "Biochimica et Biophysica Acta-Bioenergetics",

issn = "0005-2728",

publisher = "Elsevier Science B.V., Inc",

number = "2",

}

Messias, AC, Aguiar, AP, Brennan, L , Salgueiro, CA , Saraiva, LM, Xavier, AV & Turner, DL 2006, 'Solution structures of tetrahaem ferricytochrome c₃ from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity', Biochimica et Biophysica Acta-Bioenergetics, vol. 1757, no. 2, pp. 143-153. https://doi.org/10.1016/j.bbabio.2006.01.007

Solution structures of tetrahaem ferricytochrome c₃ from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity. / Messias, Ana C.; Aguiar, António P.; Brennan, Lorraine et al.
In: Biochimica et Biophysica Acta-Bioenergetics, Vol. 1757, No. 2, 02.2006, p. 143-153.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant

T2 - The molecular basis of cooperativity

AU - Messias, Ana C.

AU - Aguiar, António P.

AU - Brennan, Lorraine

AU - Salgueiro, Carlos A.

AU - Saraiva, Lígia M.

AU - Xavier, António V.

AU - Turner, David L.

PY - 2006/2

Y1 - 2006/2

N2 - The NMR structure of the oxidised wild-type cytochrome c3 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.

AB - The NMR structure of the oxidised wild-type cytochrome c3 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.

KW - Cytochrome c

KW - Multihaem cytochromes

KW - NMR

KW - Redox proteins

KW - Tetrahaem cytochrome c

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U2 - 10.1016/j.bbabio.2006.01.007

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M3 - Article

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SN - 0005-2728

VL - 1757

SP - 143

EP - 153

JO - Biochimica et Biophysica Acta-Bioenergetics

JF - Biochimica et Biophysica Acta-Bioenergetics

IS - 2

ER -

Solution structures of tetrahaem ferricytochrome c₃ from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity

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