Methanol dehydrogenase (cytochrome c)

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Methanol dehydrogenase (cytochrome c)
4mae.jpg
Methanol dehydrogenase homodimer, Methylacidiphilum fumariolicum
Identifiers
EC no.1.1.2.7
CAS no.37205-43-9
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Methanol dehydrogenase (cytochrome c) (EC 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 cL an aldehyde + 2 ferrocytochrome cL + 2 H+

A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.

References[edit]

  1. ^ Anthony C, Zatman LJ (September 1964). "The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27". The Biochemical Journal. 92 (3): 614–21. doi:10.1042/bj0920614. PMC 1206111. PMID 4378696.
  2. ^ Anthony C, Zatman LJ (September 1967). "The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". The Biochemical Journal. 104 (3): 960–9. doi:10.1042/bj1040960. PMC 1271238. PMID 6049934.
  3. ^ Duine JA, Frank J, Verwiel PE (1980). "Structure and activity of the prosthetic group of methanol dehydrogenase". European Journal of Biochemistry. 108 (1): 187–92. doi:10.1111/j.1432-1033.1980.tb04711.x. PMID 6250827.
  4. ^ Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature. 280 (5725): 843–4. doi:10.1038/280843a0. PMID 471057.
  5. ^ Cox JM, Day DJ, Anthony C (February 1992). "The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1119 (1): 97–106. doi:10.1016/0167-4838(92)90240-E. PMID 1311606.
  6. ^ Blake CC, Ghosh M, Harlos K, Avezoux A, Anthony C (February 1994). "The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues". Nature Structural Biology. 1 (2): 102–5. doi:10.1038/nsb0294-102. PMID 7656012.
  7. ^ Xia ZX, He YN, Dai WW, White SA, Boyd GD, Mathews FS (January 1999). "Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution". Biochemistry. 38 (4): 1214–20. doi:10.1021/bi9822574. PMID 9930981.
  8. ^ Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C (August 2001). "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)". Biochemistry. 40 (33): 9799–809. doi:10.1021/bi002932l. PMID 11502173.
  9. ^ Anthony C, Williams P (April 2003). "The structure and mechanism of methanol dehydrogenase". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647 (1–2): 18–23. doi:10.1016/S1570-9639(03)00042-6. PMID 12686102.
  10. ^ Williams PA, Coates L, Mohammed F, Gill R, Erskine PT, Coker A, Wood SP, Anthony C, Cooper JB (January 2005). "The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens". Acta Crystallographica Section D. 61 (Pt 1): 75–9. doi:10.1107/S0907444904026964. PMID 15608378.

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