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. (C) 2006 Elsevier B.V. All rights reserved.
Salgueiro, C. A. G., Teixeira, L. R., & 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-Bioenergetics, 1757(2), 143-153. https://doi.org/10.1016/j.bbabio.2006.01.007