H cluster hydrogenase. Jul 13, 2020 · Abstract [FeFe]-hydrogenase enzymes employ a unique organometallic cofactor for efficient and reversible hydrogen conversion. rsc. Jan 24, 2014 · The active site of FeFe hydrogenase, the H-cluster, is assembled with the help of accessory protein HydG. The active site of the diiron hydrogenase is known as the H-cluster. Jun 27, 2024 · Further application of this semisynthesis strategy shows that an [Fe 2 (SCH 2 NH 2) 2 (CO) 4 (CN) 2] 2- complex can activate the apo hydrogenase, marking it as the last biosynthetic intermediate en route to the H-cluster. Kuchenreuther et al. Fe–S cluster enzymes HydG, HydE, and HydF provide sequential assembly of the catalytic H-cluster of [FeFe] hydrogenase. The catalytic core of the [FeFe]-hydrogenase (HydA), called the H-cluster, exists as a [4Fe4S] subcluster linked to Feb 10, 2005 · Here we report the assembly of the iron-sulphur framework of the active site of iron-only hydrogenase (the H-cluster), and show that it functions as an electrocatalyst for proton reduction. The H-cluster consists of a [4Fe4S] cubane-shaped structure, coupled to the low valent diiron co-factor by a cysteine derived thiol. 1–4 These hydrogenase enzymes . This site, the H-cluster, is a six-iron ensemble consisting of a [4Fe-4S] H cluster linked to a [2Fe] H cluster that is coordinated to CO, cyanide, and a unique organic azadithiolate ligand. provide evidence into the initial steps in this synthesis. Jul 13, 2020 · The in vitro assembly of the H-cluster starting from purified [FeFe]-hydrogenase (apo-HydA1 carrying only the [4Fe–4S] cluster) and a synthetic diiron complex ( [2Fe] adt) has been probed by EPR, FTIR, and X-ray absorption spectroscopy. See full list on pubs. Jun 27, 2024 · For more than a decade, we have worked on the biosynthesis of the active site of [FeFe] hydrogenases. Apr 25, 2010 · Hydrogen metabolism is facilitated by the activity of three hydrogenase enzymes. Introduction to [FeFe] hydrogenase Hydrogenase enzymes catalyze the redox interconversion of protons and electrons with molecular hydrogen, with both [FeFe] and [NiFe] variants playing important metabolic roles in their host organisms. May 13, 2025 · [FeFe]-Hydrogenases are structurally diverse enzymes that catalyze reversible H 2 activation at a catalytic cofactor or H-cluster. 1. The H-cluster is a [4Fe-4S] cubane linked by a cysteine thiolate to a diiron subsite containing unique CO, CN -, and dithiomethylamine ligands. This so-called H-cluster consists of a [4Fe–4S] cubane cysteine linked to a diiron complex coordinated by carbon monoxide and cyanide ligands and an azadithiolate ligand (adt = NH(CH2S)2)·[FeFe]-hydrogenase apo-protein binding only the [4Fe–4S] sub-complex can be Further application of this semisynthesis strategy shows that an [Fe2(SCH2NH2)2(CO)4(CN)2]2− complex can activate the apo hydrogenase, marking it as the last biosynthetic intermediate en route to the H-cluster. org This report provides the first example of cell-free H-cluster synthesis and hydrogenase activation using individually expressed maturases, and it also clearly details the origin of all five H-cluster CO and CN − ligands. Three Fe–S “maturase” proteins, HydE, HydF, and HydG, are responsible for the biosynthesis of the [2Fe] H subcluster and its incorporation into the hydrogenase enzyme to form this catalytically active H-cluster. This combined enzymatic and semisynthetic approach greatly accelerates our understanding of H-cluster biosynthesis. k0heb wu7 bu 7yt20l trn n7vo 6g g9j ya4yb pv9