Catalytic properties of cytochrome c oxidase purified from Nitrosomonas europaea.
Cytochrome c oxidase of Nitrosomonas europaea reacts with not only the native cytochrome c (N. europaea cytochrome c-552) but also horse and yeast cytochromes c. The effects on its reactivity of various reagents were very different between the reactions with the native and eukaryotic cytochromes c as the electron donors. The oxidation of eukaryotic ferrocytochrome c by the oxidase was activated by addition of anionic detergents such as sodium dodecyl sulfate and sodium cholate, and anionic phospholipids such as cardiolipin, phosphatidylserine, phosphatidylinositol, and phosphatidylethanolamine, while the reaction was not activated by Triton X-100, Tween 20, or phosphatidylcholine. However, the reaction with the native cytochrome c of the enzyme was hardly affected by any of the detergents and phospholipids mentioned above, while it was activated by the presence of poly-L-lysine.
Yamazaki
T
T
Department of Life Science, Faculty of Science, Tokyo Institute of Technology.
Fukumori
Y
Y
Yamanaka
T
T
D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D003902:Detergents / Q000494:pharmacology; D003576:Electron Transport Complex IV / Q000378:metabolism*; D009606:Nitrosomonas / Q000201:enzymology*; D010084:Oxidation-Reduction; D010743:Phospholipids / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology
D003902:Detergents; D010743:Phospholipids; D011107:Polylysine; D003576:Electron Transport Complex IV