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The assignment of the 655 nm spectral band of cytochrome oxidase
Author(s) -
Mitchell Roy,
Mitchell Peter,
Rich Peter R.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80321-s
Subject(s) - chemistry , redox , redox titration , formate , heme , cytochrome c oxidase , cytochrome , titration , photochemistry , hemeprotein , chloride , ferric , analytical chemistry (journal) , inorganic chemistry , biochemistry , enzyme , chromatography , organic chemistry , catalysis
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 a 3 , which exhibits strong redox interaction and a titration range at significantly lower potential. Thus, although the total reduced‐oxidised difference spectrum of haem a 3 , 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 a 3 , which is modulated by the redox state of Cu B , as suggested by Beinert et al. [(1976) Biochim. Biophys. Acta 423, 339–355].