EC Number   |
Inhibitors |
Structure  |
|---|
   1.14.18.3 | more |
no detectable iron |
 |
| 1.14.18.3 | more |
inhibitor docking study, computational simulation of the structure and mechanism, modeling, overview |
|
| 1.14.18.3 | Zn2+ |
effects of zinc binding on pMMO in membrane extracts, binding efficiency varies under different consitions, multisite inhibition, detailed overview. Addition of copper to these zinc-loaded membranes results in loss of half the zinc ions |
  |
| 1.14.18.3 | Zn2+ |
zinc inhibits enzyme pMMO at two sites that are distinct from the copper active site, zinc might inhibit proton transfer in pMMO. Locations for the two zinc inhibition sites: the first is the crystallographic zinc site in the pmoC subunit, a second zinc site is present on the cytoplasmic side of the pmoC subunit |
|
| 1.14.18.3 | EDTA |
18.1% residual activity at 1.5 mM |
|
| 1.14.18.3 | H2O2 |
reversible inhibition of pMMO with H2O2 upon treatment of pMMO with H2O2 followed by the addition of catalase. H2O2 re-oxidizes the type 2 copper in pMMO reduced with duroquinol |
|
| 1.14.18.3 | Fe2+ |
slightly, membrane-bound enzyme form |
|
| 1.14.18.3 | Fe2+ |
0.75 to two iron ions per protomer. Di-iron may be the pMMO active site |
|
| 1.14.18.3 | NaCl |
decrease in activity might be due to reduced enzyme solubility with increasing NaCl concentrations |
|
| 1.14.18.3 | cyanide |
less than 2% residual activity at 2 mM |
|
