Protein Variants | Comment | Organism |
---|---|---|
A110C | mutant designed to block the CO-migrating tunnel in the alpha-subunit. Electron paramagnetic resonance spectra indicates that the A-cluster is properly assembled. ACS activity is similar to that of the wild-type recombinant Ni-activated alpha-subunit | Moorella thermoacetica |
A222L | mutant designed to block the CO-migrating tunnel in the alpha-subunit. Electron paramagnetic resonance spectra indicates that the A-cluster is properly assembled. ACS activity is similar to that of the wild-type recombinant Ni-activated alpha-subunit | Moorella thermoacetica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | binding of Ni to the A-cluster slows the reduction kinetics of the [Fe4S4]2+ cubane. An upper limit of two electrons per a subunit are transferred from titanium(III) citrate to the Ni subcomponent of the A-cluster during reductive activation. These electrons are accepted quickly relative to the reduction of the [Fe4S4]2+ cubane. This reduction is probably a prerequisite for methyl group transfer | Moorella thermoacetica | |
Nickel | binding of Ni to the A-cluster slows the reduction kinetics of the [Fe4S4]2+ cubane. An upper limit of two electrons per a subunit are transferred from titanium(III) citrate to the Ni subcomponent of the A-cluster during reductive activation. These electrons are accepted quickly relative to the reduction of the [Fe4S4]2+ cubane. This reduction is probably a prerequisite for methyl group transfer | Moorella thermoacetica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Moorella thermoacetica | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] | CO migrates to the A-cluster through two pathways, one involving and one not involving the tunnel | Moorella thermoacetica |