Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1943861 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2006 | 11 Pages |
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.
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Authors
Ana C. Messias, António P. Aguiar, Lorraine Brennan, Carlos A. Salgueiro, Lígia M. Saraiva, António V. Xavier, David L. Turner,