Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR)
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- 作者：Binuraj R.K. Menon ; Samantha J.O. Hardman ; Nigel S. Scrutton ; nigel.scrutton@manchester.ac.uk" class="auth_mail" title="E-mail the corresponding author ; Derren J. Heyes ; Derren.Heyes@manchester.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：Protochlorophyllide oxidoreductase (POR) ; Light activation ; Photochemistry ; Site-directed mutagenesis ; Enzyme catalysis
- 刊名：Journal of Photochemistry and Photobiology B: Biology
- 出版年：2016
- 出版时间：August 2016
- 年：2016
- 卷：161
- 期：Complete
- 页码：236-243
- 全文大小：2578 K
文摘
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Identified several active site residues that can interact with coenzyme/substrate
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Multiple residues are important in excited state POR–protochlorophyllide interactions.
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New structural model for T. elongatus POR to rationalize mutagenesis outcomes
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POR active site geometry is finely-tuned to support photochemistry.
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