EC Number   |
Metals/Ions |
Reference |
|---|
    1.17.98.4 | Molybdenum |
contains molybdenum |
742756 |
| 1.17.98.4 | Se |
formate dehydrogenase H contains selenocysteine as an integral amino acid. Selenium of formate dehydrogenase H is directly involved in formate oxidation |
701023 |
| 1.17.98.4 | Se |
Mo of the molybdopterin is coordinated with the Se atom of selenocysteine |
701024 |
| 1.17.98.4 | Se |
selenocysteine is located at amino acid position 140 |
695650 |
| 1.17.98.4 | Se |
selenocysteine-containing enzyme. The molybdenum-coordinated selenocysteine is essential for catalytic activity of the native enzyme |
698704 |
| 1.17.98.4 | Se |
selenocysteine-containing polypeptide |
701021 |
| 1.17.98.4 | Se |
the enzyme contains selenocysteine |
698686 |
| 1.17.98.4 | Se |
the enzyme contains selenocysteine. The Mo-Se bond is estimated to be covalent to the extent of 17-27% of the unpaired electron spin density residing in the valence 4s and 4p selenium orbitals, based on comparison of the scalar and dipolar hyperfine components to atomic 77Se. Two electron oxidation of formate by the Mo(VI) state converts Mo to the reduced Mo(IV) state with the formate proton, H+(formate), transferring to a nearby base Y-. Transfer of one electron to the Fe4S4 center converts Mo(IV) to the EPR detectable Mo(V) state. The Y- is located within magnetic contact to the [Mo-Se] center, as shown by its strong dipolar 1Hf hyperfine couplings. Photolysis of the formate-induced Mo(V) state abolishes the 1Hf hyperfine splitting from YH(formate), suggesting photoisomerization of this group or phototransfer of the proton to a more distant proton acceptor group A-. The minor effect of photolysis on the 77Se-hyperfine interaction with [77Se] selenocysteine suggests that the Y- group is not the Se atom, but instead might be the imidazole ring of the His141 residue which is located in the putative substrate-binding pocket close to the [Mo-Se] center. It is proposed that the transfer of H+(formate) from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2 |
696191 |
| 1.17.98.4 | Se |
the enzyme contains selenocysteine.The trxB gene is required for the formation of selenocysteine containing FDHH polypeptide |
687454 |
| 1.17.98.4 | Se |
the fdhF gene of Escherichia coli codes for the selenocysteine-including protein subunit of formate dehydrogenase H |
700262 |
