"Peroxidatic" form of cytochrome oxidase as studied by X-ray absorption spectroscopy.
X-ray absorption spectroscopy shows pulsed oxidase to be similar to resting oxidase but to lack the sulfur bridge between iron and copper of active sites (Powers, L., Y. Ching, B. Chance, and B. Muhoberac, 1982, Biophys. J., 37[2, Pt. 2]: 403a. [Abstr.] ) The first shell ligands and bond lengths of the pulsed oxidase active site heme most clearly fit the ferric peroxidases from horseradish and yeast, and the pulsed oxidase cyanide compound resembles the low spin hemoprotein cyanide compounds. The structural results are consistent with an aquo or a peroxo form for pulsed oxidase as is also observed by optical studies. These structural and chemical data are consistent with a role for the pulsed forms in a cyclic peroxidatic side reaction in which the pulsed and pulsed peroxide compounds act as peroxide scavengers. The peroxidatic role of cytochrome oxidase in the nonsulfur bridged form suggests the renaming of the "oxygenated" or "pulsed" forms on a functional basis as "peroxidatic" forms of cytochrome oxidase.
D055598:Chemical Phenomena; D002621:Chemistry; D003300:Copper / Q000032:analysis; D003486:Cyanides; D003576:Electron Transport Complex IV; D007501:Iron / Q000032:analysis; D007700:Kinetics; D010100:Oxygen; D010544:Peroxidases; D010545:Peroxides / Q000378:metabolism; D011789:Quantum Theory; D013057:Spectrum Analysis; D014965:X-Rays
D003486:Cyanides; D010545:Peroxides; D003300:Copper; D007501:Iron; D010544:Peroxidases; D003576:Electron Transport Complex IV; D010100:Oxygen