title: Spectroscopic characterization of the key catalytic intermediate Ni-C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride.
abstract: Ni-C in the O(2)-tolerant hydrogenase I from Aquifex aeolicus binds a hydride weaker than that in O(2)-sensitive hydrogenases. This is in line with the enhanced light-sensitivity of Ni-C, greater lability of the hydride complex and increased catalytic redox potentials relevant to bio-H(2) oxidation.
authors.affiliation: Max-Planck-Institut für Bioanorganische Chemie, Stiftstr. 34-36, 45470 Mülheim/Ruhr, Germany.
authors.forename: Maria-Eirini
authors.initials: ME
authors.lastname: Pandelia
authors.forename: Pascale
authors.initials: P
authors.lastname: Infossi
authors.forename: Matthias
authors.initials: M
authors.lastname: Stein
authors.forename: Marie-Thérèse
authors.initials: MT
authors.lastname: Giudici-Orticoni
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Lubitz
mesh_terms: D001419:Bacteria / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry*; D002244:Carbon / Q000737:chemistry; D002384:Catalysis; D004578:Electron Spin Resonance Spectroscopy; D006864:Hydrogenase / Q000737:chemistry*; D009532:Nickel / Q000737:chemistry; D010100:Oxygen / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D001426:Bacterial Proteins; D002244:Carbon; D009532:Nickel; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010100:Oxygen