title: H-cluster assembly during maturation of the [FeFe]-hydrogenase.
abstract: The organometallic H-cluster at the active site of the [FeFe]-hydrogenase serves as the site of reversible binding and reduction of protons to produce H2. The H-cluster is unique in biology, and consists of a 2Fe subcluster tethered to a typical [4Fe-4S] cluster by a single cysteine ligand. The remaining ligands to the 2Fe subcluster include three carbon monoxides, two cyanides, and a dithiomethylamine. This mini-review will focus on the significant advances in recent years in understanding the pathway for H-cluster biosynthesis, as well as the structures, roles, and mechanisms of the three enzymes directly involved.
authors: Department of Chemistry & Biochemistry, Montana State University, Bozeman, MT, 59717, USA, jbroderick@chemistry.montana.edu.
authors: Joan B
authors: JB
authors: Broderick
authors: Amanda S
authors: AS
authors: Byer
authors: Kaitlin S
authors: KS
authors: Duschene
authors: Benjamin R
authors: BR
authors: Duffus
authors: Jeremiah N
authors: JN
authors: Betz
authors: Eric M
authors: EM
authors: Shepard
authors: John W
authors: JW
authors: Peters
mesh_terms: D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular
chemical_list: D007506:Iron-Sulfur Proteins; C118830:iron hydrogenase; D006864:Hydrogenase