EC Number   |
Cofactor |
Reference |
|---|
   1.1.2.7 | 2,7,9-tricarboxypyrroloquinoline quinone |
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview |
689818 |
| 1.1.2.7 | cytochrome cL |
- |
667721, 684666, 684948, 690794, 753048 |
| 1.1.2.7 | cytochrome cL |
electron acceptor |
684950 |
| 1.1.2.7 | cytochrome cL |
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding and crystal structure determination and analysis at 1.6 A resolution, contains a disulfide bridge that tethers the long C-terminal extension to the body of the structure, overview |
688333 |
| 1.1.2.7 | cytochrome cL |
Ma-CytcL, contains heme c and has unique features compared to those of the terrestrial homologues. Apart from Fe2+ in heme, three additional metal ion binding sites for Na+, Ca2+, and Fe2+ are found, wherein the ions mostly form coordination bonds with the amino acid residues on the loop (G93-Y111) that interacts with heme. These ions seem to enhance the stability of heme insertion by increasing the loop's steadiness. The basic N-terminal end, together with helix alpha4 and loop G126-Y136, contributes positive charge to the region. In contrast, the acidic C-terminal end provides a negatively charged surface, yielding several electrostatic contact points with partner proteins for electron transfer. The need for an adapter protein bridging MDH to CytcL within appropriate proximity for electron transfer is satisfied by protein MxaJ. Native Ma-CytcL is purified from Methylophaga aminisulfidivorans cell culture by anion exchange chromatography and gel filtration. It contains a signal peptide, sequence comparisons and metal binding sites analysis, overview |
763357 |
| 1.1.2.7 | cytochrome cL |
UniProt ID A3FJ50 |
763672 |
| 1.1.2.7 | heme c |
coordination in CtcL at the active site, structure, overview. Contains Fe2+ |
763357 |
| 1.1.2.7 | heme c |
part of cytochrome cL |
688333 |
| 1.1.2.7 | more |
an NAD(P)-independent enzyme |
684948, 690794 |
| 1.1.2.7 | more |
Ma-MxaJ contains the bi-lobate folding architecture found in periplasmic binding proteins (PDB ID 5SV6), presence of an acidic cavity at the interface of the two domains |
763357 |
