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利用过渡金属配合物作为光敏剂,通过烯还原酶对α,β-不饱和化合物进行光驱动生物催化还原。

Light-driven biocatalytic reduction of α,β-unsaturated compounds by ene reductases employing transition metal complexes as photosensitizers.

作者信息

Peers Martyn K, Toogood Helen S, Heyes Derren J, Mansell David, Coe Benjamin J, Scrutton Nigel S

机构信息

Manchester Institute of Biotechnology , Faculty of Life Sciences , University of Manchester , 131 Princess Street , Manchester , M1 7DN , UK . Email:

School of Chemistry , University of Manchester , Oxford Road , Manchester , M13 9PL , UK.

出版信息

Catal Sci Technol. 2016 Jan 7;6(1):169-177. doi: 10.1039/c5cy01642h. Epub 2015 Oct 26.

DOI:10.1039/c5cy01642h
PMID:27019691
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4786955/
Abstract

Efficient and cost effective nicotinamide cofactor regeneration is essential for industrial-scale bio-hydrogenations employing flavin-containing biocatalysts such as the Old Yellow Enzymes. A direct flavin regeneration system using visible light to initiate a photoredox cycle and drive biocatalysis is described, and shown to be effective in driving biocatalytic activated alkene reduction. Using Ru(ii) or Ir(iii) complexes as photosensitizers, coupled with an electron transfer mediator (methyl viologen) and sacrificial electron donor (triethanolamine) drives catalytic turnover of two Old Yellow Enzymes with multiple oxidative substrates. Therefore, there is great potential in the development of light-driven biocatalytic systems, providing an alternative to the reliance on enzyme-based cofactor regeneration systems.

摘要

对于采用含黄素生物催化剂(如老黄色酶)的工业规模生物氢化反应而言,高效且经济高效的烟酰胺辅因子再生至关重要。本文描述了一种直接的黄素再生系统,该系统利用可见光启动光氧化还原循环并驱动生物催化反应,且已证明其在驱动生物催化活化烯烃还原反应中有效。使用钌(II)或铱(III)配合物作为光敏剂,结合电子转移介质(甲基紫精)和牺牲电子供体(三乙醇胺),可驱动两种老黄色酶对多种氧化底物的催化周转。因此,光驱动生物催化系统的开发具有巨大潜力,为依赖基于酶的辅因子再生系统提供了一种替代方案。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/7d9f031d4675/c5cy01642h-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/39dbb4d9bc1c/c5cy01642h-s1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/e81c4eb3dc4e/c5cy01642h-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/b59f35be4bd7/c5cy01642h-s2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/65099b52f822/c5cy01642h-s3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/7d9f031d4675/c5cy01642h-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/39dbb4d9bc1c/c5cy01642h-s1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/e81c4eb3dc4e/c5cy01642h-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/b59f35be4bd7/c5cy01642h-s2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/65099b52f822/c5cy01642h-s3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1abe/4786955/7d9f031d4675/c5cy01642h-f2.jpg

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