EC Number   |
Cofactor |
Reference |
|---|
   1.17.5.3 | bis(molybdopterin guanine dinucleotide)molybdenum cofactor |
the structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 A through the enzyme. In the catalytic site, the Mo directly takes up electrons from the bound substrate. These electrons are transferred to the beta subunit through the [4Fe4S] cluster (FeS-0) in the alpha subunit. The four [4Fe-4S] clusters in the beta subunit, which are aligned in the order of FeS-1, FeS-4, FeS-2, and FeS-3, connect the alpha and gamma subunits like an electric wire. From FeS-3 of the beta subunit, electrons are transferred to heme bP (P for periplasm) in the gamma subunit and then across the membrane to heme bC (C for cytoplasm). Menaquinone binds to a histidine ligand (Hisg169) of heme bC and can directly accept electrons through this residue |
677117 |
| 1.17.5.3 | cytochrome b |
the low-potential cytochrome b of the formate dehydrogenase complex is an essential component in the electron transport from formate to menaquinone. The 25000 Da subunit represents cytochrome b |
390364 |
| 1.17.5.3 | cytochrome b556 |
FdnI encodes cytochrome b556 |
698688 |
| 1.17.5.3 | heme |
the enzyme contains (in relative molar amounts): 1.0 heme, 0.95 molybdenum, 0.96 selenium, 14 non-heme iron, and 13 acid-labile sulfide |
698681 |
| 1.17.5.3 | heme b |
the structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 A through the enzyme. In the catalytic site, the Mo directly takes up electrons from the bound substrate. These electrons are transferred to the beta subunit through the [4Fe4S] cluster (FeS-0) in the alpha subunit. The four [4Fe-4S] clusters in the beta subunit, which are aligned in the order of FeS-1, FeS-4, FeS-2, and FeS-3, connect the alpha and gamma subunits like an electric wire. From FeS-3 of the beta subunit, electrons are transferred to heme bP (P for periplasm) in the gamma subunit and then across the membrane to heme bC (C for cytoplasm). Menaquinone binds to a histidine ligand (Hisg169) of heme bC and can directly accept electrons through this residue |
677117 |
| 1.17.5.3 | menaquinone |
the structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 A through the enzyme. In the catalytic site, the Mo directly takes up electrons from the bound substrate. These electrons are transferred to the beta subunit through the [4Fe4S] cluster (FeS-0) in the alpha subunit. The four [4Fe-4S] clusters in the beta subunit, which are aligned in the order of FeS-1, FeS-4, FeS-2, and FeS-3, connect the alpha and gamma subunits like an electric wire. From FeS-3 of the beta subunit, electrons are transferred to heme bP (P for periplasm) in the gamma subunit and then across the membrane to heme bC (C for cytoplasm). Menaquinone binds to a histidine ligand (Hisg169) of heme bC and can directly accept electrons through this residue |
677117 |
| 1.17.5.3 | molybdopterin |
- |
741271 |
