4KN9

High-resolution structure of H2-activated anaerobically purified Dm. baculatum [NiFeSe]-hydrogenase after crystallization under air

Summary for 4KN9

Entry DOI	10.2210/pdb4kn9/pdb
Related	1CC1 4KL8 4KO1 4KO2 4KO3 4KO4
Descriptor	Periplasmic [NiFeSe] hydrogenase small subunit, Nickel-dependent hydrogenase large subunit, IRON/SULFUR CLUSTER, ... (10 entities in total)
Functional Keywords	o2-resistance, h2 cleavage/production, nifese-site, oxidoreductase
Biological source	Desulfomicrobium baculatum More
Cellular location	Periplasm: P13063
Total number of polymer chains	4
Total formula weight	175583.49
Authors	Volbeda, A.,Cavazza, C.,Fontecilla-Camps, J.C. (deposition date: 2013-05-09, release date: 2013-07-10, Last modification date: 2024-11-20)
Primary citation	Volbeda, A.,Amara, P.,Iannello, M.,De Lacey, A.L.,Cavazza, C.,Fontecilla-Camps, J.C. Structural foundations for the O2 resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenase. Chem.Commun.(Camb.), 49:7061-7063, 2013 Cited by PubMed Abstract: This study shows how the NiFeSe site of an anaerobically purified O2-resistant hydrogenase reacts with air to give a seleninate as the first product. Less oxidized states of the active site are readily reduced in the presence of X-rays. Reductive enzyme activation requires an efficient pathway for water escape. PubMed: 23811828 DOI: 10.1039/c3cc43619e PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.4 Å)

Structure validation