[Electron transport in hemoproteins. VIII. The effect of chemical modification of ferricytochrome C on the rate of its reduction by oxymyoglobin].
The influence of chemical modification of separate amino acid residues in ferricytochrome c (Cyt c) on the rate of the redox reaction with MbO2 has been studied at various pH and ionic strength values. It is shown that alkylation of His-33 and Met-65 by bromacetate does not affect the reaction rate. On the contrary, acylation of Tyr-74 or one of the neighbouring lysines, Lys-72 or Lys-73, by the spin-label N-(2,2',5,5'-tetramethyl-3-carboxypyrrolin-1-oxy)-imidazol diminishes sharply the efficiency of electron transfer in the redox system studied. Besides, unlike the reaction between native proteins, the rate of electron transfer in this case does not depend on ionic strength. The modification of Tyr-74 or Lys 72/43 does not alter the midpoint potential and the entire conformation of Cyt c. The observed effects can therefore be explained by essential disturbance of interactions, first of all, the electrostatic ones in the active complex, which is induced by the attachment of the bulky reagent to the site of "active contact" of Cyt c. Based on the obtained findings and the atomic coordinates of Cyt c, the positions of all charge and some uncharged groups on the surface of Cyt c interacting with myoglobin during electron transfer are presented.
D000818:Animals; D001665:Binding Sites; D002850:Chromatography, Gel; D003574:Cytochrome c Group / Q000032:analysis / Q000378:metabolism*; D004579:Electron Transport; D006418:Heme / Q000378:metabolism*; D007700:Kinetics; D008745:Methylation; D009132:Muscles / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism*; D010084:Oxidation-Reduction; D013113:Spin Labels; D013552:Swine; D014907:Whales
D003574:Cytochrome c Group; D009211:Myoglobin; D013113:Spin Labels; C017595:oxymyoglobin; D006418:Heme
Izuchenie perenosa élektrona v gemoproteinakh. VIII. Vliianie khimicheskoĭ modifikatsii ferritsitokhroma C na skorost' vosstanovleniia ego oksimioglobinom.