Focusing on a nickel hydrocorphinoid in a protein matrix: methane generation by methyl-coenzyme M reductase with F430 cofactor and its models
Focusing on a nickel hydrocorphinoid in a protein matrix: methane generation by methyl-coenzyme M reductase with F430 cofactor and its models
复制标题
聚焦蛋白质基质中的镍类氢化蛇蝎：带有 F430 辅因子的甲基辅酶 M 还原酶产生甲烷及其模型
DOI：
10.1039/d1cs00840d
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发表时间：
2022
影响因子：
46.2
通讯作者：
Hayashi Takashi
中科院分区：
文献类型：
--
作者：
Miyazaki Yuta;Oohora Koji;Hayashi Takashi
甲基辅酶M还原酶（MCR）是催化厌氧甲烷生成和氧化的一种重要酶，它含有一个氢化corphoid镍辅因子F430。MCR中的活性Ni(I)将甲基辅酶M （CH3S-CoM）和辅酶B （HS-CoB）转化为甲烷和杂二硫化物（CoM-S-S-CoB）。广泛的实验和理论研究集中在MCR中的底物结合腔，包括F430辅因子，已经提出了两种主要不同的反应机制，涉及有机镍CH3-Ni （III）物种或瞬时甲基自由基物种。在对天然MCR本身进行研究的同时，MCR的功能也在F430模型复合物和最近基于蛋白质的功能模型（包括镍配合物）的背景下进行了研究。在后一种情况下，已经发现用四氢和二脱氢类角质镍配合物重构的血红蛋白代表了负责甲烷生成的有用模型系统。这些努力支持了酶促反应的机制，并为复制mcr样甲烷生成过程提供了重要的见解。此外，本文描述的MCR模型有望导致对蛋白质支持的镍卟啉类化学的理解，以及MCR激发催化的创造。
Methyl-coenzyme M reductase (MCR) containing a nickel hydrocorphinoid cofactor, F430, is an essential enzyme that catalyzes anaerobic methane generation and oxidation. The active Ni(I) species in MCR converts methyl-coenzyme M (CH3S–CoM) and coenzyme B (HS–CoB) to methane and heterodisulfide (CoM–S–S–CoB). Extensive experimental and theoretical studies focusing on the substrate-binding cavity including the F430 cofactor in MCR have suggested two principally different reaction mechanisms involving an organonickel CH3–Ni(III) species or a transient methyl radical species. In parallel with research on native MCR itself, the functionality of MCR has been investigated in the context of model complexes of F430 and recent protein-based functional models, which include a nickel complex. In the latter case, hemoproteins reconstituted with tetradehydro- and didehydrocorrinoid nickel complexes have been found to represent useful model systems that are responsible for methane generation. These efforts support the proposed mechanism of the enzymatic reaction and provide important insight into replicating the MCR-like methane-generation process. Furthermore, the modeling of MCR described here is expected to lead to understanding of protein-supported nickel porphyrinoid chemistry as well as the creation of MCR-inspired catalysis.