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Literature summary for 1.3.7.7 extracted from

  • Silva, P.J.
    With or without light comparing the reaction mechanism of dark-operative protochlorophyllide oxidoreductase with the energetic requirements of the light-dependent protochlorophyllide oxidoreductase (2014), PeerJ, 2, e551 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus P26164 subunit bchN
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Rhodobacter capsulatus ATCC BAA-309 P26164 subunit bchN
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process Rhodobacter capsulatus ?
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additional information The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process Rhodobacter capsulatus ATCC BAA-309 ?
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Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center reaction potential of the Fe–S cluster shows pH-dependence Rhodobacter capsulatus