7O1T

Fe(CO)2CNCl species bound [HydE from T. Maritima

Summary for 7O1T

• Entry DOI: 10.2210/pdb7o1t/pdb
• Descriptor: [FeFe] hydrogenase maturase subunit HydE, CHLORIDE ION, IODIDE ION, ... (12 entities in total)
• Functional Keywords: radical sam protein; hydrogenase maturase; metalloprotein, metal binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 42993.63

Authors

Rohac, R.,Martin, L.,Liu, L.,Basu, D.,Tao, L.,Britt, R.D.,Rauchfuss, T.,Nicolet, Y. (deposition date: 2021-03-30, release date: 2021-05-26, Last modification date: 2024-01-31)

Primary citation

Rohac, R.,Martin, L.,Liu, L.,Basu, D.,Tao, L.,Britt, R.D.,Rauchfuss, T.B.,Nicolet, Y.
Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B.
J.Am.Chem.Soc., 143:8499-8508, 2021

PubMed Abstract: [FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H into protons and low-potential electrons. It can be best described as a [FeS] cluster coupled to a unique [2Fe] 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-CH-NH-CH-S) and an additional bridging CO. This [2Fe] 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)CN 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)CN" precursor to the [2Fe] center. Substrate access, product release, and intermediate transfer are also discussed.

PubMed: 34048236
DOI: 10.1021/jacs.1c03367

Experimental method

X-RAY DIFFRACTION (1.5 Å)