The assignment of the 655 nm spectral band of cytochrome oxidase.
The spectral characteristics of the '655 nm' band of cytochrome oxidase were found to be affected by ligands of the binuclear centre, including formate and chloride, and by the resting/pulsed transition. The band titrated with near n = 1 characteristics at a midpoint of about 400 mV, in contrast to haem a3, which exhibits strong redox interaction and a titration range at significantly lower potential. Thus, although the total reduced-oxidised difference spectrum of haem a3 shows a trough at about 655 nm, this characteristic is absent in the low potential region. The 655 nm feature may arise from a charge transfer band of ferric high-spin haem a3, which is modulated by the redox state of CuB, as suggested by Beinert et al. [(1976) Biochim. Biophys. Acta 423, 339-355].
Mitchell
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Glynn Research Institute, Bodmin, UK.
Mitchell
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Rich
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D000818:Animals; D002417:Cattle; D002712:Chlorides / Q000737:chemistry; D003300:Copper / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D005561:Formates / Q000737:chemistry; D006418:Heme / Q000031:analogs & derivatives / Q000737:chemistry; D008024:Ligands; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D013053:Spectrophotometry
D002712:Chlorides; D005561:Formates; D008024:Ligands; C030544:formic acid; C027728:heme a; D006418:Heme; D003300:Copper; D003576:Electron Transport Complex IV