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Literature summary extracted from

  • Bodo, G.; Branca, R.M.; Toth, A.; Horvath, D.; Bagyinka, C.
    Concentration-dependent front velocity of the autocatalytic hydrogenase reaction (2009), Biophys. J., 96, 4976-4983.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.12.99.6 additional information front velocity increases as the overall enzyme concentration (and hence the concentration of the autocatalyst form of the enzyme) is increased Thiocapsa roseopersicina

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.99.6 additional information front velocity decreases on increase of the electron acceptor benzyl viologen concentration at all measured hydrogenase concentrations Thiocapsa roseopersicina

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.99.6 Fe the electron acceptor interacts only with the [FeS]distal cluster in the hydrogenase, and accordingly the autocatalyst is a hydrogenase form in which the [FeS]distal cluster holds an electron (i.e., at least the [FeS]distal cluster is reduced) Thiocapsa roseopersicina

Organism

EC Number Organism UniProt Comment Textmining
1.12.99.6 Thiocapsa roseopersicina
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.99.6 partially and fully purified Thiocapsa roseopersicina

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.99.6 H2 + oxidized benzyl viologen
-
 Thiocapsa roseopersicina H+ + reduced benzyl viologen
-
 ?
1.12.99.6 additional information hydrogenase during its reaction cycle has an autocatalytic step Thiocapsa roseopersicina ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.12.99.6 HynSL hydrogenase
-
 Thiocapsa roseopersicina
1.12.99.6 [NiFe] hydrogenase
-
 Thiocapsa roseopersicina