[Electron transfer to hemoproteins. II. pH-dependence of the reduction rate of ferricytochrome c by oxymyoglobin].
The pH-dependence of the reduction rate of ferricytochrome C by intact and chemically modified oxymyoglobins has been studied. The modification was performed with respect to histidine residues and alpha-aminogroup of N-terminal valine. Two histidine residues of myoglobin, His A10 and His GH1, are shown to take part in the realization of the "active" contact between the molecules in the course of the reaction. The deprotonation of the first residue contributes to the acceleration and that of the second to the reduction of the reaction. The found orientation of the Mb molecules in the "active complex" implies that at any orientation of cytochrome C the distance between the haemes of the both molecules should be more than 30 A. This makes highly probable that a structure-dependent mechanism of electron transfer in the system under study can be proposed.
D001665:Binding Sites; D003574:Cytochrome c Group; D004579:Electron Transport; D006420:Hemeproteins; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D009211:Myoglobin; D010084:Oxidation-Reduction; D011487:Protein Conformation
D003574:Cytochrome c Group; D006420:Hemeproteins; D009211:Myoglobin
Izuchenie perenosa élektrona v gemoproteinakh. II. Zavisimost-skorosti vosstanovleniia ferritsitokhroma c oksimioglobinom ot pH.