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Literature summary for 1.12.99.6 extracted from

  • Hartmann, S.; Frielingsdorf, S.; Ciaccafava, A.; Lorent, C.; Fritsch, J.; Siebert, E.; Priebe, J.; Haumann, M.; Zebger, I.; Lenz, O.
    O2-tolerant H2 activation by an isolated large subunit of a [NiFe] hydrogenase (2018), Biochemistry, 57, 5339-5349 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Cupriavidus necator 16020
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
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SDS-PAGE, large subunit HoxG Cupriavidus necator

Organism

Organism UniProt Comment Textmining
Cupriavidus necator
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Cupriavidus necator HF795
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Oxidation Stability

Oxidation Stability Organism
the enzyme is O2 tolerant Cupriavidus necator

Purification (Commentary)

Purification (Comment) Organism
purification of large subunit preHoxG Cupriavidus necator

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the large subunit preHoxG is able to activate H2 as it performs catalytic hydrogen/deuterium exchange. However, it did not execute the entire catalytic cycle described for [NiFe] hydrogenases. H2 activation is performed by preHoxG even in the presence of O2, although the unique [4Fe-3S] cluster located in the small subunit and described to be crucial for tolerance toward O2 is absent Cupriavidus necator ?
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additional information the large subunit preHoxG is able to activate H2 as it performs catalytic hydrogen/deuterium exchange. However, it did not execute the entire catalytic cycle described for [NiFe] hydrogenases. H2 activation is performed by preHoxG even in the presence of O2, although the unique [4Fe-3S] cluster located in the small subunit and described to be crucial for tolerance toward O2 is absent Cupriavidus necator HF795 ?
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Cofactor

Cofactor Comment Organism Structure
[4Fe-3S]-center the unique [4Fe-3S] cluster is located in the small subunit Cupriavidus necator