1giw
SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE
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OverviewOverview
In the frame of a broad study on the structural differences between the, two redox forms of cytochromes to be related to the electron transfer, process, the NMR solution structure of horse heart cytochrome c in the, reduced form has been determined. The structural data obtained in the, present work are compared to those already available in the literature on, the same protein and the presence of conformational differences is, discussed in the light of the experimental method employed for the, structure determination. Redox-state dependent changes are analyzed and in, particular they are related to the role of propionate-7 of the heme. Also, some hydrogen bonds are changed upon reduction of the heme iron. A, substantial similarity is observed for the backbone fold, independently of, the oxidation state. At variance, some meaningful differences are observed, in the orientation of a few side chains. These changes are related to, those found in the case of the highly homologous cytochrome c from, Saccharomyces cerevisiae. The exchangeability of the NH protons has been, investigated and found to be smaller than in the case of the oxidized, protein. We think that this is a characteristic of reduced cytochromes and, that mobility is a medium for molecular recognition in vivo.
About this StructureAbout this Structure
1GIW is a Single protein structure of sequence from Equus caballus with HEC as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of reduced horse heart cytochrome c., Banci L, Bertini I, Huber JG, Spyroulias GA, Turano P, J Biol Inorg Chem. 1999 Feb;4(1):21-31. PMID:10499099
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