1FEH

FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM

Summary for 1FEH

• Entry DOI: 10.2210/pdb1feh/pdb
• Descriptor: PROTEIN (PERIPLASMIC HYDROGENASE 1), 2 IRON/2 SULFUR/5 CARBONYL/2 WATER INORGANIC CLUSTER, IRON/SULFUR CLUSTER, ... (5 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Clostridium pasteurianum
• Total number of polymer chains: 1
• Total formula weight: 65849.42

Authors

Peters, J.W.,Lanzilotta, W.N.,Lemon, B.J.,Seefeldt, L.C. (deposition date: 1998-10-28, release date: 1999-01-13, Last modification date: 2024-02-07)

Primary citation

Peters, J.W.,Lanzilotta, W.N.,Lemon, B.J.,Seefeldt, L.C.
X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
Science, 282:1853-1858, 1998

PubMed Abstract: A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined to 1.8 angstrom resolution by x-ray crystallography using multiwavelength anomalous dispersion (MAD) phasing. CpI, an enzyme that catalyzes the two-electron reduction of two protons to yield dihydrogen, was found to contain 20 gram atoms of iron per mole of protein, arranged into five distinct [Fe-S] clusters. The probable active-site cluster, previously termed the H-cluster, was found to be an unexpected arrangement of six iron atoms existing as a [4Fe-4S] cubane subcluster covalently bridged by a cysteinate thiol to a [2Fe] subcluster. The iron atoms of the [2Fe] subcluster both exist with an octahedral coordination geometry and are bridged to each other by three non-protein atoms, assigned as two sulfide atoms and one carbonyl or cyanide molecule. This structure provides insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.

PubMed: 9836629
DOI: 10.1126/science.282.5395.1853

Experimental method

X-RAY DIFFRACTION (1.8 Å)