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Literature summary extracted from

  • Loescher, S.; Burgdorf, T.; Zebger, I.; Hildebrandt, P.; Dau, H.; Friedrich, B.; Haumann, M.
    Bias from H2 cleavage to production and coordination changes at the Ni-Fe active site in the NAD+-reducing hydrogenase from Ralstonia eutropha (2006), Biochemistry, 45, 11658-11665.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.12.1.2 H16L in the HoxH-mutant protein H16L, H2 oxidation is impaired, but H2 production occurrs via a stable Ni-C state (N(III)-(H-)-Fe(II)) Cupriavidus necator

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.1.2 Fe Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover Cupriavidus necator
1.12.1.2 Ni Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover Cupriavidus necator

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.12.1.2 H2 + NAD+ Cupriavidus necator the enzyme catalyzes electron transfer from molecular hydrogen to NAD+, thereby producing reducing equivalents for CO2 fixation in the form of NADH H+ + NADH
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Organism

EC Number Organism UniProt Comment Textmining
1.12.1.2 Cupriavidus necator
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.1.2 H2 + NAD+
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 Cupriavidus necator H+ + NADH
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1.12.1.2 H2 + NAD+ the enzyme catalyzes electron transfer from molecular hydrogen to NAD+, thereby producing reducing equivalents for CO2 fixation in the form of NADH Cupriavidus necator H+ + NADH
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