7o1t | pdb_00007o1t
Fe(CO)2CNCl species bound [HydE from T. Maritima
Structural highlights
Function[HYDE_THEMA] Required for the maturation of the [FeFe]-hydrogenase HydA (By similarity). Catalyzes the reductive cleavage of S-adenosyl-L-methionine (in vitro), suggesting it may contribute to the biosynthesis of an essential sulfur-containing ligand that binds to the hydrogenase active site [2Fe-2S] cluster (PubMed:16137685).[UniProtKB:Q97IK9][1] Publication Abstract from PubMed[FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H2 into protons and low-potential electrons. It can be best described as a [Fe4S4] cluster coupled to a unique [2Fe]H center where the reaction actually takes place. The latter corresponds to two iron atoms, each of which is bound by one CN(-) ligand and one CO ligand. The two iron atoms are connected by a unique azadithiolate molecule ((-)S-CH2-NH-CH2-S(-)) and an additional bridging CO. This [2Fe]H center is built stepwise thanks to the well-orchestrated action of maturating enzymes that belong to the Hyd machinery. Among them, HydG converts l-tyrosine into CO and CN(-) to produce a unique l-cysteine-Fe(CO)2CN species termed complex-B. Very recently, HydE was shown to perform radical-based chemistry using synthetic complex-B as a substrate. Here we report the high-resolution crystal structure that establishes the identity of the complex-B-bound HydE. By triggering the reaction prior to crystallization, we trapped a new five-coordinate Fe species, supporting the proposal that HydE performs complex modifications of complex-B to produce a monomeric "SFe(CO)2CN" precursor to the [2Fe]H center. Substrate access, product release, and intermediate transfer are also discussed. Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B.,Rohac R, Martin L, Liu L, Basu D, Tao L, Britt RD, Rauchfuss TB, Nicolet Y J Am Chem Soc. 2021 Jun 9;143(22):8499-8508. doi: 10.1021/jacs.1c03367. Epub 2021, May 28. PMID:34048236[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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