E. coli Nickel-Iron Hydrogenase 1 Catalyses Non-native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme Ene-reductases**
E. coli Nickel-Iron Hydrogenase 1 Catalyses Non-native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme Ene-reductases**
复制标题
大肠杆菌镍铁氢化酶 1 催化黄素的非天然还原：老黄酶烯还原酶对烯烃氢化的演示**
DOI：
10.1002/ange.202101186
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发表时间：
2021
影响因子：
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通讯作者：
Joseph Srinivasan S
中科院分区：
文献类型：
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作者：
Joseph Srinivasan S
本文报道了大肠杆菌（Escherichia coli，Hyd 1）[NiFe]摄取氢化酶1的一种新活性。生物黄素辅因子FMN和FAD的直接还原使用H2作为简单的、完全原子经济的还原剂来实现。Hyd 1的稳定性被用于在广泛的温度范围（25-70 °C）和延长的反应时间内还原黄素。该系统作为一种简单、易于实施的FMNH 2或FADH 2再生系统的实用性随后通过向Old Yellow酶“烯还原酶”提供还原的黄素以支持高达100%转化率的不对称烯烃还原来证明。在黄素回收过程中，Hyd 1的周转频率高达20.4 min-1，总周转次数高达20200。
A new activity for the [NiFe] uptake hydrogenase 1 of Escherichia coli (Hyd1) is presented. Direct reduction of biological flavin cofactors FMN and FAD is achieved using H2as a simple, completely atom‐economical reductant. The robust nature of Hyd1 is exploited for flavin reduction across a broad range of temperatures (25–70 °C) and extended reaction times. The utility of this system as a simple, easy to implement FMNH2or FADH2regenerating system is then demonstrated by supplying reduced flavin to Old Yellow Enzyme “ene‐reductases” to support asymmetric alkene reductions with up to 100 % conversion. Hyd1 turnover frequencies up to 20.4 min−1and total turnover numbers up to 20 200 were recorded during flavin recycling.