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

FEBS Letters

Nugent, Jonathan P²  Townley, Helen E¹  Griffiths, W.Trevor¹ 

[1] Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK;Department of Biology, University College London, Gower Street, London WC1E 6BT, UK

关键词: Protochlorophyllide reductase;    Photoenzyme mechanism;    Radical intermediate;    Flavoenzyme;    mbp-por;    maltose binding protein fusion of protochlorophyllide oxidoreductase;    IPTG;    isopropyl-β-d-galactoside;   

DOI  :  10.1016/S0014-5793(97)01589-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown