EC Number   |
Metals/Ions |
Reference |
|---|
   1.14.13.25 | Iron |
the diiron active site of each homodimer is located in the alpha subunit, and no other metal centers are present. The resting state active site (MMOHox) consists of two Fe(III) ions coordinated by Glu114, His147, and a solvent molecule (Fe1), and Glu209, Glu243, and His246 (Fe2). The iron ions are 3.1 A apart, coordinated in pseudooctahedral fashion and bridged by two solvent molecules as well as Glu144 |
745389 |
| 1.14.13.25 | more |
does not require Cu2+ |
671477 |
| 1.14.13.25 | more |
sMMO activity and expression does not require Cu2+ |
701759 |
| 1.14.13.25 | more |
sMMO contains no metal ions |
438950 |
| 1.14.13.25 | more |
the enzyme contains very low or no amounts of copper and zinc |
672690 |
| 1.14.13.25 | more |
the enzyme does not contain and require Cu2+ for activity |
745389 |
| 1.14.13.25 | more |
the soluble methane monooxygenase contains no copper |
745730 |
| 1.14.13.25 | NaCl |
as a true halotolerant enzyme, MmoC still shows 50% of its specific activity at 2 M NaCl. Evaluation of salt tolerance for NADH-mediated reduction of benzyl viologen by MmoC at non-optima conditions, 23°C and pH 7.0 |
764485 |
| 1.14.13.25 | Ni2+ |
protein B contains 0.04 mol Ni2+ per mol protein |
438930 |
| 1.14.13.25 | Zn2+ |
0.2-0.5 mol zinc per mol protein |
438931 |
