Publication Abstract from PubMed
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.
Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: the molecular basis of cooperativity.,Messias AC, Aguiar AP, Brennan L, Salgueiro CA, Saraiva LM, Xavier AV, Turner DL Biochim Biophys Acta. 2006 Feb;1757(2):143-53. Epub 2006 Feb 20. PMID:16527248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
