Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View

被引:11
作者
Nicolet, Yvain [1 ]
Cherrier, Mickael V. [1 ]
Amara, Patricia [1 ]
机构
[1] Univ Grenoble Alpes, CNRS, Metalloproteins Unit, CEA,IBS, F-38000 Grenoble, France
来源
ACS BIO & MED CHEM AU | 2022年 / 2卷 / 01期
关键词
Nitrogenase; FeFe]-hydrogenase; X-ray crystallography; Metalloproteins; Iron-sulfur; clusters; Radicals; Active site assembly; NITROGENASE FEMO-COFACTOR; PARAMAGNETIC-RESONANCE CHARACTERIZATION; IRON-MOLYBDENUM COFACTOR; IN-VITRO SYNTHESIS; CRYSTAL-STRUCTURE; INTERSTITIAL ATOM; ONLY HYDROGENASE; ACTIVE-SITE; H-CLUSTER; FUNCTIONAL-CHARACTERIZATION;
D O I
10.1021/acsbiomedchemau.1c00044
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This Review focuses on the structure-function relationship of radical S-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.
引用
收藏
页码:36 / 52
页数:17
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