[Study of electron transfer in hemoproteins. IV. Oxidation of sperm whale oxymoglobin catalyzed by copper ions].
The influence of cupric ions on the oxidation of sperm whale oxymoglobin and soybean oxyleghemoglobin at pH 4.8--7.5 and 10--40 degrees C has been studied. The stability constants of cupric ions to myoglobin were determined: K1 = 3.4 . 10(5) M(-1) for the more reactive center, and K2 = 2.1 . 10(3) M(-1) for the next 5--7 binding centers. The role of ionization of His-GH1 in the process of oxidation of sperm whale myoglobin is discussed. A mechanism of electron transfer from myoglobin molecule to the external acceptor is presented.
D000818:Animals; D002384:Catalysis; D002591:Cetacea / Q000378:metabolism*; D003300:Copper; D004579:Electron Transport; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007874:Leghemoglobin; D009211:Myoglobin / Q000302:isolation & purification; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013025:Glycine max / Q000032:analysis; D013696:Temperature; D014907:Whales / Q000378:metabolism*
D007874:Leghemoglobin; D009211:Myoglobin; C017595:oxymyoglobin; D003300:Copper
Izuchenie perenosa élektrona v gemoproteinakh. IV. Kataliziruemoe ionami medi okislenie oksimioglobina kashalota.