A reappraisal of the mechanism of the photoenzyme protochlorophyllide reductase based on studies with the heterologously expressed protein

被引：21
|
作者：
Townley, HE
Griffiths, WT [1 ]
Nugent, JP
机构：
[1] Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England
[2] Univ London Univ Coll, Dept Biol, London WC1E 6BT, England
来源：
FEBS LETTERS | 1998年 / 422卷 / 01期
关键词：
protochlorophyllide reductase; photoenzyme mechanism; radical intermediate; flavoenzyme;
D O I：
10.1016/S0014-5793(97)01589-5
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：
It is widely believed that protochlorophyllide reductase is a flavoenzyme effecting catalysis by a radical mechanism. Here the cyanobacterial reductase has been isolated from Escherichia coli overexpressing the Synechocystis gene, The purified enzyme, while retaining full activity, has no detectable flavine. No radical derived ESR signal was observed during catalysis or on photoexcitation under non-catalytic conditions, Mechanistic implications of the findings are discussed. (C) 1998 Federation of European Biochemical Societies.
引用
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页码：19 / 22
页数：4
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