By J D Dunitz

ISBN-10: 354009816X

ISBN-13: 9783540098164

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1 to 2 seconds after mixing and Fmd intense high and low spin Fo(III) signals. The combined intensity accounts for as much as 80% or more of all the iron in the oxidase. Thus the high spin signal, or at least the major rhombic component must be uncoupled high spin Fe(III) in heine a~ +. Whether or not the a~ + is magnetically isolated because the EPR invisible copper is still reduced is not clear. Addition of 02 causes a rapid decrease in the g = 6 sigua1145). Of course the EPR silent copper is crucial to the arguments summarized, and on this point, Hu, Chan and Brown have presented a serious challenge 15o,lSl).

But in the last few years there have been a considerable number of reports providing some evidence for the presence of intermotaUic interactions in this enzyme which allow for its inclusion at this time. It is generally accepted that cytochxome oxidase contains two heeos and two copper ions. Although the two iron porphyrins are identical, heeo A11°,119), they are inoquivalent in spectra and functional behavior in the oxidase. A. Cohen binding for CO and CN-. For example CO inhibits the oxidation of home a3 but not that of home a whereas CN- likewise interferes with the reduction of home a a but not that of home & In addition to binding of CO, CN- and N~, current interest has been directed toward inhibition of the oxidase by formate 122,12a), sulfide 124,12s) and NO12S).

There is no evidence for the liberation of intermediate oxidation states of oxygen such as peroxide or superoxide. The presence of two homes and two coppers has lead to the assumption (but not without some strong exception, vide infra) that all four metal ions are involved in the red-ox process. The partial red-ox reactions of the oxidase in the presence of CO is a good example of an unresolved dispute regarding the number of metal ions participating in the reaction. The binding of only one CO per oxidase molecule (to heine as) in the reduced state has been confirmed by infrared studies 12a) and it is well known that heme aa oxidation is inhibited by CO.

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Biochemistry by J D Dunitz

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