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Literature summary extracted from

  • Long, H.; King, P.W.; Ghirardi, M.L.; Kim, K.
    Hydrogenase/ferredoxin charge-transfer complexes: effect of hydrogenase mutations on the complex association (2009), J. Phys. Chem. A, 113, 4060-4067.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.12.7.2 D102K leads to lower binding free energies and higher association rate with [2Fe2S]-ferredoxin FDX1 and is thus a promising target for improving hydrogen production rates in engineered organisms Chlamydomonas reinhardtii
1.12.7.2 D102K/E221K double mutant enhances association rate constant Chlamydomonas reinhardtii
1.12.7.2 D102K/T99K double mutant enhances association rate constant Chlamydomonas reinhardtii
1.12.7.2 E221K higher association rate with [2Fe2S]-ferredoxin FDX1 Chlamydomonas reinhardtii
1.12.7.2 M214K least enhancement of association rate with [2Fe2S]-ferredoxin FDX1, destabilizes binding complexes Chlamydomonas reinhardtii
1.12.7.2 T99K leads to lower binding free energies and higher association rate with [2Fe2S]-ferredoxin FDX1 and is thus a promising target for improving hydrogen production rates in engineered organisms Chlamydomonas reinhardtii

Organism

EC Number Organism UniProt Comment Textmining
1.12.7.2 Chlamydomonas reinhardtii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.7.2 H2 + oxidized ferredoxin
-
Chlamydomonas reinhardtii reduced ferredoxin + 2 H+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.12.7.2 HydA2
-
Chlamydomonas reinhardtii
1.12.7.2 [FeFe]-hydrogenase
-
Chlamydomonas reinhardtii

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.7.2 Ferredoxin
-
Chlamydomonas reinhardtii