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| Name = Methanol dehydrogenase (cytochrome c)
| EC_number = 1.1.2.7
| CAS_number = 37205-43-9
| IUBMB_EC_number = 1/1/2/7
| GO_code =
| image =
| width =
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}}Methanol dehydrogenase (cytochrome c) ({{EC number|1.1.2.7}}, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase.[1][2][3][4][5][6][7][8][9][10] This enzyme catalyses the following chemical reaction
a primary alcohol + 2 ferricytochrome cLan aldehyde + 2 ferrocytochrome cL + 2 H+
A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.
References
1. ^{{cite journal | title = The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27 |author1 = Anthony, C. |author2 =Zatman, L.J. |journal = Biochem. J. |year = 1964 |volume = 92 |pages = 614–621 |pmid = 4378696 |issue=3 |pmc=1206111}}
2. ^{{cite journal | title = The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group |author1 = Anthony, C. |author2 =Zatman, L.J. |journal = Biochem. J. |year = 1967 |volume = 104 |pages = 960–969 |pmid = 6049934 |issue=3 |pmc=1271238}}
3. ^{{cite journal | title = Structure and activity of the prosthetic group of methanol dehydrogenase |author1 = Duine, J.A. |author2 =Frank, J. |author3 =Verweil, P.E.J. |journal = Eur. J. Biochem. |year = 1980 |volume = 108 |pages = 187–192 |pmid = 6250827 |issue=1 |doi=10.1111/j.1432-1033.1980.tb04711.x}}
4. ^{{cite journal | title = A novel coenzyme from bacterial primary alcohol dehydrogenases |author1 = Salisbury, S.A. |author2 =Forrest, H.S. |author3 =Cruse, W.B.T. |author4 =Kennard, O. |journal = Nature |year = 1979 |volume = 280 |pages = 843–844 |pmid = 471057 |issue=5725 |doi=10.1038/280843a0}}
5. ^{{cite journal | title = The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria |author1 = Cox, J.M. |author2 =Day, D.J. |author3 =Anthony, C. |journal = Biochim. Biophys. Acta |year = 1992 |volume = 1119 |pages = 97–106 |pmid = 1311606 |doi=10.1016/0167-4838(92)90240-E}}
6. ^{{cite journal | title = The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues |author1 = Blake, C.C. |author2 =Ghosh, M. |author3 =Harlos, K. |author4 =Avezoux, A. |author5 =Anthony, C. |journal = Nat. Struct. Biol. |year = 1994 |volume = 1 |pages = 102–105 |pmid = 7656012 |issue=2 |doi=10.1038/nsb0294-102}}
7. ^{{cite journal | title = Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution |author1 = Xia, Z.X. |author2 =He, Y.N. |author3 =Dai, W.W. |author4 =White, S.A. |author5 =Boyd, G.D. |author6 =Mathews, F.S. | journal = Biochemistry |year = 1999 |volume = 38 |pages = 1214–1220 |pmid = 9930981 |doi=10.1021/bi9822574 |issue=4}}
8. ^{{cite journal | title = Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL |author1 = Afolabi, P.R. |author2 =Mohammed, F. |author3 =Amaratunga, K. |author4 =Majekodunmi, O. |author5 =Dales, S.L. |author6 =Gill, R. |author7 =Thompson, D. |author8 =Cooper, J.B. |author9 =Wood, S.P. |author10 =Goodwin, P.M. |author11 =Anthony, C. | journal = Biochemistry |year = 2001 |volume = 40 |pages = 9799–9809 |pmid = 11502173 |issue=33 |doi=10.1021/bi002932l}}
9. ^{{cite journal | title = The structure and mechanism of methanol dehydrogenase |author1 = Anthony, C. |author2 =Williams, P. |journal = Biochim. Biophys. Acta |year = 2003 |volume = 1647 |pages = 18–23 |pmid = 12686102 |doi=10.1016/S1570-9639(03)00042-6}}
10. ^{{cite journal | title = The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens |author1 = Williams, P.A. |author2 =Coates, L. |author3 =Mohammed, F. |author4 =Gill, R. |author5 =Erskine, P.T. |author6 =Coker, A. |author7 =Wood, S.P. |author8 =Anthony, C. |author9 =Cooper, J.B. | journal = Acta Crystallogr. D |year = 2005 |volume = 61 |pages = 75–79 |pmid = 15608378 |doi=10.1107/S0907444904026964 |issue=Pt 1}}
2. ^{{cite journal | title = The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group |author1 = Anthony, C. |author2 =Zatman, L.J. |journal = Biochem. J. |year = 1967 |volume = 104 |pages = 960–969 |pmid = 6049934 |issue=3 |pmc=1271238}}
3. ^{{cite journal | title = Structure and activity of the prosthetic group of methanol dehydrogenase |author1 = Duine, J.A. |author2 =Frank, J. |author3 =Verweil, P.E.J. |journal = Eur. J. Biochem. |year = 1980 |volume = 108 |pages = 187–192 |pmid = 6250827 |issue=1 |doi=10.1111/j.1432-1033.1980.tb04711.x}}
4. ^{{cite journal | title = A novel coenzyme from bacterial primary alcohol dehydrogenases |author1 = Salisbury, S.A. |author2 =Forrest, H.S. |author3 =Cruse, W.B.T. |author4 =Kennard, O. |journal = Nature |year = 1979 |volume = 280 |pages = 843–844 |pmid = 471057 |issue=5725 |doi=10.1038/280843a0}}
5. ^{{cite journal | title = The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria |author1 = Cox, J.M. |author2 =Day, D.J. |author3 =Anthony, C. |journal = Biochim. Biophys. Acta |year = 1992 |volume = 1119 |pages = 97–106 |pmid = 1311606 |doi=10.1016/0167-4838(92)90240-E}}
6. ^{{cite journal | title = The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues |author1 = Blake, C.C. |author2 =Ghosh, M. |author3 =Harlos, K. |author4 =Avezoux, A. |author5 =Anthony, C. |journal = Nat. Struct. Biol. |year = 1994 |volume = 1 |pages = 102–105 |pmid = 7656012 |issue=2 |doi=10.1038/nsb0294-102}}
7. ^{{cite journal | title = Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution |author1 = Xia, Z.X. |author2 =He, Y.N. |author3 =Dai, W.W. |author4 =White, S.A. |author5 =Boyd, G.D. |author6 =Mathews, F.S. | journal = Biochemistry |year = 1999 |volume = 38 |pages = 1214–1220 |pmid = 9930981 |doi=10.1021/bi9822574 |issue=4}}
8. ^{{cite journal | title = Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL |author1 = Afolabi, P.R. |author2 =Mohammed, F. |author3 =Amaratunga, K. |author4 =Majekodunmi, O. |author5 =Dales, S.L. |author6 =Gill, R. |author7 =Thompson, D. |author8 =Cooper, J.B. |author9 =Wood, S.P. |author10 =Goodwin, P.M. |author11 =Anthony, C. | journal = Biochemistry |year = 2001 |volume = 40 |pages = 9799–9809 |pmid = 11502173 |issue=33 |doi=10.1021/bi002932l}}
9. ^{{cite journal | title = The structure and mechanism of methanol dehydrogenase |author1 = Anthony, C. |author2 =Williams, P. |journal = Biochim. Biophys. Acta |year = 2003 |volume = 1647 |pages = 18–23 |pmid = 12686102 |doi=10.1016/S1570-9639(03)00042-6}}
10. ^{{cite journal | title = The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens |author1 = Williams, P.A. |author2 =Coates, L. |author3 =Mohammed, F. |author4 =Gill, R. |author5 =Erskine, P.T. |author6 =Coker, A. |author7 =Wood, S.P. |author8 =Anthony, C. |author9 =Cooper, J.B. | journal = Acta Crystallogr. D |year = 2005 |volume = 61 |pages = 75–79 |pmid = 15608378 |doi=10.1107/S0907444904026964 |issue=Pt 1}}
External links
- {{MeshName|Methanol+dehydrogenase+(cytochrome+c)}}
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