[Effect of ligand orientation on the redox potential of homologous proteins].
Using experimental g-values of homologous cytochromes isolated from the horse heart and bacterial cyt-c-551 from Pseudomonas aeruginosa, the electron energy difference of redox-orbital of Fe(III) ion of heme was calculated during reduction. Data are in a good accordance with experimental redox-potential values for these proteins. The model gives opportunity to predict redox-potential values for other homologous proteins.
D000818:Animals; D001426:Bacterial Proteins; D003574:Cytochrome c Group / Q000032:analysis*; D004578:Electron Spin Resonance Spectroscopy; D006736:Horses; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D013045:Species Specificity
D001426:Bacterial Proteins; D003574:Cytochrome c Group; C017167:cytochrome C(551)
Vliianie orientatsii ligandov na redoks-potentsial gomologichnykh belkov.