Fe-only Hydrogenase (Larger Subunit); Chain L, domain 3
CYS 34;CYS 46;CYS 49;CYS 62(2Fe-2S cluster)
HIS 94;CYS 98;CYS 101;CYS 107(4Fe-4S cluster-1)
CYS 300;CYS 499(4Fe-4S cluster-4 [H-cluster]);CYS 503(4Fe-4S cluster-4 & diiron [2Fe] subcluster [H-cluster])
Purification and properties of the H2-oxidizing (uptake) hydrogenase of the N2-fixing anaerobe Clostridium pasteurianum W5.
The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I.
Mossbauer and electron nuclear double resonance study of oxidized bidirectional hydrogenase from Clostridium pasteurianum W5.
On the novel H2-activating iron-sulfur center of the "Fe-only" hydrogenases.
Mossbauer study of Clostridium pasteurianum hydrogenase II. Evidence for a novel three-iron cluster.
X-ray-absorption-spectroscopic evidence for a novel iron cluster in hydrogenase II from Clostridium pasteurianum.
Immunological relationship among hydrogenases.
Electron paramagnetic resonance studies of the low temperature photolytic behavior of oxidized hydrogenase I from Clostridium pasteurianum.
Magnetic circular dichroism and electron paramagnetic resonance studies of hydrogenases I and II from Clostridium pasteurianum.
Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum.
The structure and mechanism of iron-hydrogenases.
Primary structure of hydrogenase I from Clostridium pasteurianum.
Resonance Raman studies of iron-only hydrogenases.
Heterologous biosynthesis and characterization of the [2Fe-2S]-containing N-terminal domain of Clostridium pasteurianum hydrogenase.
Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli.
Biological hydrogen production: not so elementary.
X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum.
Structure and mechanism of iron-only hydrogenases.
Reversible carbon monoxide binding and inhibition at the active site of the Fe-only hydrogenase.
A novel FeS cluster in Fe-only hydrogenases.
A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a low-energy route for heterolytic cleavage and formation of dihydrogen.
Coordination sphere flexibility of active-site models for Fe-only hydrogenase: studies in intra- and intermolecular diatomic ligand exchange.
Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: examination of its light sensitivity at cryogenic temperatures.
Hydrogenases: hydrogen-activating enzymes.
DFT investigation of structural, electronic, and catalytic properties of diiron complexes related to the [2Fe](H) subcluster of Fe-only hydrogenases.
Fe-only hydrogenases: structure, function and evolution.
Density functional theory investigation of the active site of [Fe]-hydrogenases: effects of redox state and ligand characteristics on structural, electronic, and reactivity properties of complexes related to the [2Fe]H subcluster.
The organometallic active site of [Fe]hydrogenase: models and entatic states.
Hydrogenases: active site puzzles and progress.
Enzymatic mechanism of Fe-only hydrogenase: density functional study on H-H making/breaking at the diiron cluster with concerted proton and electron transfers.
A semi-empirical molecular orbital scheme to study electron transfer in iron-sulphur proteins.
Combined spectroscopic/computational study of binuclear Fe(I)-Fe(I) complexes: implications for the fully-reduced active-site cluster of Fe-only hydrogenases.
Synthetic chemistry: making a natural fuel cell.
Synthesis of the H-cluster framework of iron-only hydrogenase.
This enzyme belongs to Fe-only hydrogenases. This enzyme is homologous to [Fe] hydrogenase (or DdH) (M00012 in EzCatDB). iomethyl)amine and 5 cyanide or carbon monoxide molecules. Although this enzyme is homologous to DdH (M00012), the direction of electron transfer is opposite to the counpterpart enzyme, DdH (see M00012). This enzyme binds five cofactors, a 2FE-2S cluster, three 4Fe-4S clusters, and one H cluster. The H cluster is composed of 4Fe-4S cluster, diiron (2Fe) subcluster, bridged via a thiolate of Cys503. The diiron subcluster is liganded by 2 sulfur atoms, 1 water, and 5 cyanide or carbon monoxide molecules. According to the literature [16], this enzyme catalyzes the following reactions: (A) Electron transfer from ferredoxin to the 2Fe-2S cluster: (A') Electron transfer from ferredoxin to the 4Fe-4S cluster-1: (B) Electron transfer from the 2Fe-2S cluster to the 4Fe-4S cluster-2: (B') Electron transfer from the 4Fe-4S cluster-1 to the 4Fe-4S cluster-2: (C) Electron transfer from the 4Fe-4S cluster-2 to the 4Fe-4S cluster-3: (D) Electron transfer from the 4Fe-4S cluster-3 to the H cluster: (E) Hydrogenation (H2 production from 2 H+ ions) at H cluster: The reactions proceeds as follows (see [17]): (A') Electron transfer from ferredoxin to the 4Fe-4S cluster-1: (A'1) Indirect transfer from 2Fe-2S of ferredoxin through Cys98 bound to 4Fe-4S cluster-1. (B) Electron transfer from the 2Fe-2S cluster to the 4Fe-4S cluster-2: (B1) Indirect transfer from Cys34 bound to 2Fe-2S to Cys150 bound to 4Fe-4S cluster-2. (B') Electron transfer from the 4Fe-4S cluster-1 to the 4Fe-4S cluster-2: (B'1) Indirect transfer from His94 bound to 4Fe-4S cluster-1 to either sulfur of the 4Fe-4S cluster-2 or Cys147 through Val202. (C) Electron transfer from the 4Fe-4S cluster-2 to the 4Fe-4S cluster-3: (C1) Indirect transfer from Cys153 bound to 4Fe-4S cluster-2 to Cys196 bound to 4Fe-4S cluster-3 (probably through Met166). (D) Electron transfer from the 4Fe-4S cluster-3 to the H cluster: (D1) Indirect transfer from Cys193 bound to 4Fe-4S cluster-3 to Cys499 bound to H cluster.