PHOTOOXIDATION OF HIGH-POTENTIAL (C559, C556) AND LOW-POTENTIAL (C552) HEMES IN THE CYTOCHROME SUBUNIT OF RHODOPSEUDOMONAS-VIRIDIS REACTION CENTER - CHARACTERIZATION BY FTIR SPECTROSCOPY

被引：25

作者：

NABEDRYK, E ^{[1
]}

BERTHOMIEU, C ^{[1
]}

VERMEGLIO, A ^{[1
]}

BRETON, J ^{[1
]}

机构：

[1] CEN CADARACHE,DPVE,SBC,F-13108 ST PAUL DURANCE,FRANCE

来源：

FEBS LETTERS | 1991年 / 293卷 / 1-2期

关键词：

FOURIER TRANSFORM INFRARED SPECTROSCOPY; BACTERIAL REACTION CENTER; PHOTOSYNTHESIS; CYTOCHROME; RHODOPSEUDOMONAS-VIRIDIS;

D O I：

10.1016/0014-5793(91)81151-W

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The photooxidation of c559, c556 and c552 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.

引用

页码：53 / 58

页数：6

共 35 条

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