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Photooxidation of high‐potential ( c 559 , c 556 ) and low‐potential ( c 552 ) hemes in the cytochrome subunit of Rhodopseudomonas viridis reaction center
Author(s) -
Nabedryk E.,
Berthomieu C.,
Verméglio A.,
Breton J.
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)81151-w
Subject(s) - cytochrome c , cytochrome , chemistry , heme , photochemistry , stereochemistry , cytochrome b , protein subunit , spectroscopy , crystallography , hemeprotein , redox , biochemistry , enzyme , inorganic chemistry , physics , mitochondrion , quantum mechanics , mitochondrial dna , gene
The photooxidation of c 559 , c 556 , and c 552 hemes in Rhodopseudomonas viridis cytochrome has been characterized by light‐induced FTIR difference spectroscopy. Apart from the common features at 1659 cm −1 and 1561/1551 cm −1 which could arise from one (or possibly two) peptide bond(s), no evidence for major structural rearrangement of the polypeptide backbone was observed. A significant difference with respect to redox‐induced FTIR spectra of cytochrome c is the absence of the Tyr marker at 1514/1518 cm −1 in Rps. viridis cytochrome, indicating that the localized shift of a Tyr side chain observed between ferro‐ and ferri‐cytochrome c does not occur in Rps. viridis cytochrome.