Functional intermediates in reaction of cytochrome oxidase with oxygen.
The development of a low temperature kinetic method for the flash photolysis of the compounds of membrane-bound cytochrome a3 with carbon monoxide in the presence of oxygen affords evidence for three categories of functional intermediate compounds of cytochrome a3 and oxygen. The three classes are identified as follows: Compounds of Type A are considered to be "oxy" compounds of the ferrous heme. They have the composition a3-2+. O2. Compounds of Type B are considered to be peroxide compounds (CU-2+A3-3+ O-2= or CU-2+A3-3+ O2H2) or the equivalent heme Fe-Cu peroxide bridge structures. Compounds of Type C are formed from the ferricyanide pretreated oxidase and may involve higher oxidation states of the heme iron such as quadrivalent iron, and peroxide. Kinetic and equilibrium studies show these compounds to be functional in oxygen reduction in the sequence A yields B yield cytochromes a, c, c1, etc.
D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D010856:Columbidae; D003300:Copper / Q000032:analysis; D003576:Electron Transport Complex IV / Q000378:metabolism; D007501:Iron / Q000032:analysis; D007700:Kinetics; D008931:Mitochondria, Muscle / Q000201:enzymology; D009206:Myocardium; D010100:Oxygen; D010777:Photochemistry; D011485:Protein Binding; D013053:Spectrophotometry; D013696:Temperature; D013816:Thermodynamics
D003300:Copper; D007501:Iron; D003576:Electron Transport Complex IV; D010100:Oxygen