Nicolet Yvain, Cherrier Mickael V, Amara Patricia
Univ. Grenoble Alpes, CEA, CNRS, IBS, Metalloproteins Unit, F-38000 Grenoble, France.
ACS Bio Med Chem Au. 2021 Nov 20;2(1):36-52. doi: 10.1021/acsbiomedchemau.1c00044. eCollection 2022 Feb 16.
This Review focuses on the structure-function relationship of radical -adenosyl-l-methionine (SAM) enzymes involved in the assembly of metallocofactors corresponding to the active sites of [FeFe]-hydrogenase and nitrogenase [MoFe]-protein. It does not claim to correspond to an extensive review on the assembly machineries of these enzyme active sites, for which many good reviews are already available, but instead deals with the contribution of structural data to the understanding of their chemical mechanism (Buren et al. Chem. Rev.2020, 142 ( (25), ) 11006-11012; Britt et al. Chem. Sci.2020, 11 ( (38), ), 10313-10323). Hence, we will present the history and current knowledge about the radical SAM maturases HydE, HydG, and NifB as well as what, in our opinion, should be done in the near future to overcome the existing barriers in our understanding of this fascinating chemistry that intertwine organic radicals and organometallic complexes.
本综述聚焦于参与组装与[FeFe]-氢化酶和固氮酶[MoFe]-蛋白活性位点相对应的金属辅因子的自由基-腺苷甲硫氨酸（SAM）酶的结构-功能关系。它并非旨在全面综述这些酶活性位点的组装机制（关于这些已有许多优秀综述），而是探讨结构数据对理解其化学机制的贡献（Buren等人，《化学评论》，2020年，142卷，第25期，11006 - 11012页；Britt等人，《化学科学》，2020年，11卷，第38期，10313 - 10323页）。因此，我们将介绍关于自由基SAM成熟酶HydE、HydG和NifB的历史及当前认知，以及我们认为在不久的将来为克服现有障碍以理解这种将有机自由基与有机金属配合物交织在一起的迷人化学所应采取的措施。
