title: [Catalytic effect of ferricyanide on the rate of electron transfer between myoglobin and cytochrome c].
abstract: The influence of small amounts of low-molecular electron acceptor, potassium ferricyanide, 1 to 20% relative to the cytohrome c concentration, on the rate of electron transfer in the sperm whale oxymyoglobin--horse heart cytochrome c and deoxymyoglobin--cytochrome c systems (under aerobic and anaerobic conditions, respectively) was studied. At low ionic strength, the redox reaction rate was found to increase proportionally to the concentration of ferricyanide in both redox systems. The effect depends on pH in the pH range 5-8, increasing sharply at pH < 6. It was shown that the enhancing of electron transfer is caused by the complexing of [Fe(CN)6]3- with cytohrome c in the Lys72 region, where one of the two strong binding sites for this anion is determined by NMR. Both the high ionic strength and the chemical modification of Lys72 residue inhibit this effect at low ionic strength, markedly decreasing the rate of reaction with myoglobin. Under the same conditions, the effect of ferricyanide in the reaction of oxy-Mb with yeast cytohrome c, which is isopotential to animal cytochromes c but possesses trimethylated Lys72, was several times smaller. In turn, the chemical modification of His residues in myoglobin and the complexing of zinc ion to His119(GH1) almost completely inhibit electron transfer in the systems. Thus, electron transfer between the proteins must proceed through the formation of the Mb.[Fe(CN)6]3-.Cyt c ternary complex, the contacting sites being localized in the His119(GH1) region of myoglobin and near Lys72 of cytohrome c. The increased electron transfer rate in the presence of [Fe(CN)6]3- can be explained by that its binding near Lys72, firstly, provides better electrostatic interactions in the electron transfer complex and, besides, decreases significantly (about 2-fold) the tunneling distance between the two hemes (two lengths of 1.7 and 1.2 nm instead of one of 2.9 nm).
authors.affiliation: Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
authors.forename: S A
authors.initials: SA
authors.lastname: Moiseeva
authors.forename: G B
authors.initials: GB
authors.lastname: Postnikova
authors.forename: V S
authors.initials: VS
authors.lastname: Sivozhelezov
mesh_terms: D000085:Acetates / Q000737:chemistry; D000818:Animals; D002175:Candida / Q000737:chemistry; D002384:Catalysis; D003574:Cytochrome c Group / Q000737:chemistry*; D004579:Electron Transport; D005292:Ferricyanides / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007460:Iodoacetamide / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D009211:Myoglobin / Q000031:analogs & derivatives* / Q000737:chemistry*; D009994:Osmolar Concentration; D013113:Spin Labels; D014443:Tyrosine / Q000737:chemistry; D014907:Whales; D015032:Zinc / Q000737:chemistry
chemical_list: D000085:Acetates; D003574:Cytochrome c Group; D005292:Ferricyanides; D009211:Myoglobin; D013113:Spin Labels; C055547:deoxymyoglobin; C017595:oxymyoglobin; C007931:hexacyanoferrate III; D014443:Tyrosine; D006639:Histidine; C016274:bromoacetate; D015032:Zinc; D008239:Lysine; D007460:Iodoacetamide