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Literature summary for extracted from

  • Burgdorf, T.; Loescher, S.; Liebisch, P.; Van der Linden, E.; Galander, M.; Lendzian, F.; Meyer-Klaucke, W.; Albracht, S.P.; Friedrich, B.; Dau, H.; Haumann, M.
    Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy (2005), J. Am. Chem. Soc., 127, 576-592.
    View publication on PubMed


Metals/Ions Comment Organism Structure
Fe Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO) Cupriavidus necator
Ni Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO). The unusual ligation of the Ni by only two thiols plus further (C,O) ligands seems to be a prerequisite of the exceptionally rapid activation of the SH by NADH, involving the loss of an oxygen ligand from the Ni. Evidence for the binding of hydrogen to the open coordination site at Ni has been obtained. The hydrogen cleavage reaction seems not to involve a Ni-C state (Ni(III)-H-). The CN ligand at the Ni may be involved in establishing both rapid activation and oxygen-insensitive catalytic behavior in the SH. Possibly, one important function of the CN is stabilization of the Ni(II) oxidation state throughout the catalytic cycle of hydrogen cleavage Cupriavidus necator


Organism UniProt Comment Textmining
Cupriavidus necator

Purification (Commentary)

Purification (Comment) Organism
Cupriavidus necator

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + NAD+
Cupriavidus necator H+ + NADH


Synonyms Comment Organism
NAD-reducing hydrogenase
Cupriavidus necator