EC Number   |
Metals/Ions |
Reference |
|---|
    2.3.1.169 | CO |
a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate |
644678, 644854, 644857 |
| 2.3.1.169 | Fe |
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis |
644858 |
| 2.3.1.169 | Ni |
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis |
644858 |
| 2.3.1.169 | more |
a nucleophilic metal center on enzyme is the active site which accepts the methyl group from the methylated corrinoid/iron-sulfur protein |
644850 |
| 2.3.1.169 | Fe2+ |
a [Fe4S4] cluster |
719862 |
| 2.3.1.169 | 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 |
687824 |
| 2.3.1.169 | 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 |
687824 |
| 2.3.1.169 | Cu+ |
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex |
658436 |
| 2.3.1.169 | Ni2+ |
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex |
658436 |
| 2.3.1.169 | Zn2+ |
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex |
658436 |
