EC Number   |
Cofactor |
Reference |
|---|
   1.1.2.10 | 2,7,9-tricarboxypyrroloquinoline quinone |
Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu3+ |
762927 |
| 1.1.2.10 | cytochrome cGJ |
- |
762927 |
| 1.1.2.10 | cytochrome cGJ |
c-type cytochrome, XoxG, contains a heme-binding pocket. Recombinant expression in Escherichia coli strain BL21(DE3) and purification from periplasm, method overview. When La-, Ce-, and Nd-metalated XoxFs are assayed with XoxG as electron acceptor, the Vmax values are not significantly different for the three enzymes, but the Km for XoxG increases from 0.0025 mM for La-XoxF to 0.0076 mM for Nd-XoxF. Determination of extinction coefficients and redox potential |
763431 |
| 1.1.2.10 | cytochrome cGJ |
encoded by gene Mfumv2_1185, the cytochrome cL homologue from the strictly lanthanide-dependent, thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV is a fusion of a XoxG cytochrome and a periplasmic binding protein XoxJ. XoxGJ functions as the direct electron acceptor of its corresponding XoxF-type MDH and can sustain methanol turnover, when a secondary cytochrome is present as final electron acceptor. SolV cytochrome cGJ (XoxGJ) further displays a unique, red-shifted absorbance spectrum, with a Soret and Q bands at 440, 553 and 595 nm in the reduced state, respectively. VTVH-MCD spectroscopy reveals the presence of a low spin iron heme and the data further shows that the heme group exhibits minimal ruffling. The midpoint potential Em,pH7 of +240 mV is similar to other cytochrome cL type proteins but the midpoint potential of cytochrome cGJ is not influenced by lowering the pH. Covalently attached heme c moiety, the heme modification of SolV cytochrome cGJ, might stabilize it at lower pH and prevent the increase in midpoint potential |
762751 |
| 1.1.2.10 | cytochrome cGJ |
XoxG exhibits an unusually low reduction potential with impact on physiological methanol oxidation, XoxG crystal structure and structure-function analysis. The heme c moiety, which is covalently attached to the protein through two thioether bonds to C95 and C98 via the signature CXXCH motif for heme attachment, is enclosed in a hydrophobic pocket formed by three core alpha-helices (helices I, III, and V). This binding motif leaves one of the heme edges open to solvent. Typical of most class I c-type cytochromes, the FeIII is axially ligated by a His residue contributed by helix I (H99) and a Met residue from the loop between helices III and V (M143). Unlike most other class I cytochromes c, XoxG lacks helix IV, and this region is instead a 19-residue loop, the end of which is partially disordered. Alignment of XoxG with the cytochrome c domain and the XoxF homology model with the dehydrogenase domain suggests a plausible XoxF binding interface on XoxG. In the model, the loops between helices I and II and between III and V in XoxG are positioned to interact with XoxF. The X-ray crystal structure of XoxG is solved to 2.71 A resolution |
756461 |
| 1.1.2.10 | heme |
bound to XoxG |
763431 |
| 1.1.2.10 | pyrroloquinoline quinone |
- |
742793, 757067, 757094, 757095, 757244, 757724, 758451 |
| 1.1.2.10 | pyrroloquinoline quinone |
PQQ, PQQ is synthesized in the cytosol, but the proteins that use it are periplasmic, it might bind to subunit XoxJ near or at residue W200, no binding to XoxJ mutant W200F. Metal-bound PQQ is bound at subunit XoxF |
756461 |
| 1.1.2.10 | pyrroloquinoline quinone |
PQQ, recombinant expression and binding analysis, method overview |
763431 |
| 1.1.2.10 | pyrroloquinoline quinone |
pyrroloquinoline quinone-containing enzyme |
762947, 763273, 763388 |
