Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | tightly bound close to the inner heme propionate, Ca2+ is involved in stabilization of the redox potential, and is important in the flow of electrons from reduced pyrroloquinoline quinone in methanol dehydrogenase to the heme of cytochrome cL | Methylorubrum extorquens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | Methylorubrum extorquens | - |
formaldehyde + ferrocytochrome cL | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylorubrum extorquens | P16027 and P14775 | P16027 (large subunit, alpha) and P14775 (small subunit, beta) | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | - |
Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? | |
methanol + ferricytochrome cL | flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL | Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MDH | - |
Methylorubrum extorquens |
methanol dehydrogenase | - |
Methylorubrum extorquens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 | Methylorubrum extorquens | |
heme c | part of cytochrome cL | Methylorubrum extorquens | |
pyrroloquinoline quinone | flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure | Methylorubrum extorquens |