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Detection of a near infra‐red absorption band of ferrohaem a 3 in cytochrome c oxidase
Author(s) -
Rich Peter R.,
Moody A.John,
Ingledew W.John
Publication year - 1992
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(92)80659-5
Subject(s) - cyanide , cytochrome c oxidase , chemistry , absorption band , absorption (acoustics) , cytochrome , carbon monoxide , crystallography , photochemistry , stereochemistry , analytical chemistry (journal) , inorganic chemistry , physics , biochemistry , optics , enzyme , catalysis , organic chemistry
We have detected weak absorption bands in the near infra‐red region of reduced mammalian cytochrome c oxidase, analogous to those that we have recently reported to be present in the bacterial cytochrome o (Ingledew, W.J., Bacon, M. and Rich, P.R. (1992) FEBS Lett. 305, 167–170). The major band is centred at 784 nm and has an εmM 1 cm 1 of around 0.1. It is shifted to 760 nm in the carbon monoxide compound and is absent in the reduced cyanide complex. We attribute it to a charge transfer band of ferrohaem a 3 , equivalent to the ‘band III’ or ‘conformational band’ of haemoglobin.