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

Biochim Biophys Acta. 2006 Feb;1757(2):143-53. doi: 10.1016/j.bbabio.2006.01.007. Epub 2006 Feb 20.

Authors

Ana C Messias¹, António P Aguiar, Lorraine Brennan, Carlos A Salgueiro, Lígia M Saraiva, António V Xavier, David L Turner

Affiliation

¹ Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal.

PMID: 16527248
DOI: 10.1016/j.bbabio.2006.01.007

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Cytochrome c Group / chemistry*
Cytochrome c Group / genetics*
Desulfovibrio vulgaris / chemistry*
Desulfovibrio vulgaris / genetics*
Ferric Compounds / chemistry*
Heme / chemistry*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Oxidation-Reduction
Oxygen / administration & dosage
Oxygen / metabolism
Point Mutation
Protein Conformation
Protein Structure, Secondary
Solutions

Substances

Cytochrome c Group
Ferric Compounds
Solutions
Heme
cytochrome c(3)
Oxygen