Electron flow between photosystem II and oxygen in chloroplasts of photosystem I-deficient algae is mediated by a quinol oxidase involved in chlororespiration

被引:121
作者
Cournac, L
Redding, K
Ravenel, J
Rumeau, D
Josse, EM
Kuntz, M
Peltier, G
机构
[1] CEA, Ctr Cadarache, LEP, DEVM,DSV, F-13108 St Paul Les Durance, France
[2] Univ Alabama, Dept Chem & Coalit BioMol Prod, Tuscaloosa, AL 35487 USA
[3] CEA Cadarache, CNRS, UMR 163, DEVM,DSV, F-13108 St Paul Les Durance, France
[4] Univ Grenoble 1, CNRS, UMR 5575, Lab Genet Mol Plantes, F-38041 Grenoble 09, France
关键词
D O I
10.1074/jbc.M908732199
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
In Chlamydomonas reinhardtii mutants deficient in photosystem I because of inactivation of the chloroplast genes psaA or psaB, oxygen evolution from photosystem II occurs at significant rates and is coupled to a stimulation of oxygen uptake. Both activities can be simultaneously monitored by continuous mass spectrometry in the presence of O-18(2), The light-driven O-2 exchange was shown to involve the plastoquinone pool as an electron carrier, but not cytochrome b(6)f, Photosystem II-dependent O-2 production and O-2 uptake were observed in isolated chloroplast fractions. Photosystem II-dependent oxygen exchange was insensitive to a variety of inhibitors (azide, carbon monoxide, cyanide, antimycin A, and salicylhydroxamic acid) and radical scavengers. It was, however, sensitive to propyl gallate, From inhibitors effects and electronic requirements of the O-2 uptake process, we conclude that an oxidase catalyzing oxidation of plastoquinol and reduction of oxygen to water is present in thylakoid membranes. From the sensitivity of flash-induced O-2 exchange to propyl gallate, we conclude that this oxidase is involved in chlororespiration, Clues to the identity of the protein implied in this process are given by pharmacological and immunological similarities with a protein (IMMUTANS) identified in Arabidopsis chloroplasts.
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页码:17256 / 17262
页数:7
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