A PROTEIN CONFORMATIONAL CHANGE ASSOCIATED WITH THE PHOTOREDUCTION OF THE PRIMARY AND SECONDARY QUINONES IN THE BACTERIAL REACTION CENTER

被引：80

作者：

NABEDRYK, E

BAGLEY, KA

THIBODEAU, DL

BAUSCHER, M

MANTELE, W

BRETON, J

机构：

[1] UNIV CALIF SAN DIEGO,DEPT PHYS,LA JOLLA,CA 92093

[2] INST BIOPHYS & STRAHLENBIOL,W-7800 FREIBURG,GERMANY

来源：

FEBS LETTERS | 1990年 / 266卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

Bacterial reaction center; Fourier transform infrared spectroscopy; Photosynthesis; Primary quinone; Secondary quinone;

D O I：

10.1016/0014-5793(90)81506-J

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：

A comparison is made between the PQA → P+Q-A and PQAQB → P+QAQ-B transitions in Rps. viridis and Rb. sphaeroides reaction centers (RCs) by the use of light-induced Fourier transform infrared (FTIR) difference spectroscopy. In Rb. sphaeroides RCs, we identify a signal at 1650 cm-1 which is present in the P+QA-minus-PQA spectrum and not in the P+QAQ-B-minus-PQAQB spectrum. In contrast, this signal is present in both P+Q-A-minus-PQ-A and P+QAQ-B-minus-PQAQB spectra of Rps. viridis RCs. These data are interpreted in terms of a conformational change of the protein backbone near QA (possible at the peptide CO of a conserved alanine residue in the QA pocket) and of the different bonding interactions of QB with the protein in the RC of the two species. © 1990.

引用

页码：59 / 62

页数：4

共 16 条

[1] STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER-SPHAEROIDES R-26 - PROTEIN COFACTOR (QUINONES AND FE-2+) INTERACTIONS .5. [J].