Messias, A.C., Aguiar, A.P., Brennan, L., Salgueiro, C.A., Saraiva, L.M., Xavier, A.V. and Turner, D.L.
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), . (doi:10.1016/j.bbabio.2006.01.007).
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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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