1.1.2.7: methanol dehydrogenase (cytochrome c)
This is an abbreviated version!
For detailed information about methanol dehydrogenase (cytochrome c), go to the full flat file.
Word Map on EC 1.1.2.7
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1.1.2.7
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1.1.99.8
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phenazine
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methylamine
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formaldehyde
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hyphomicrobium
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quinoproteins
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pyrroloquinoline
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methylophilus
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denitrificans
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paracoccus
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methylotrophus
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half-reaction
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linewidth
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quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
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extorquens
- 1.1.2.7
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1.1.99.8
- phenazine
- methylamine
- formaldehyde
- hyphomicrobium
-
quinoproteins
-
pyrroloquinoline
- methylophilus
- denitrificans
-
paracoccus
- methylotrophus
-
half-reaction
-
linewidth
-
quinone-dependent
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methylobacterium
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protiated
-
wurster
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methylomonas
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one-electron
- extorquens
Reaction
+ 2 ferricytochrome cL = + 2 ferrocytochrome cL + 2 H+
Synonyms
EC 1.1.99.8, Hd-MDH, MDH, MDH2, MEDH, methanol dehydrogenase, More, mxaF, MxaJ, PQQ-dependent methanol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase, QH-ADH, QMDH, quinohemoprotein (type II) alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein dehydrogenase, quinoprotein methanol dehydrogenase, type I MDH, type II MDH
ECTree
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Crystallization
Crystallization on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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enzyme or cytochrome cL, hanging drop vapour diffusion method, 16°C, 0.001 ml of 20 mg/mL enzyme or cofactor in 40 mM Tris-HCl buffer, pH 7.5, is mixed with an equal volume of precipitant colution containing 0.2 M potassium thiocyanate and 20% PEG 3350 for the enzyme crystallization, and 2 mM ZnSO4, 20% PEG 10000, and 100 mM HEPES, pH 7.3, for the crystallization of Cyt cL, 1 week to 1 month, X-ray diffraction structure determination and analysis at 1.98-2.5 A resolution
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hanging-drop vapor diffusion method, X-ray structures of methanol dehydrogenase (Hd-MDH) and cytochrome cL at 2.5 A and 2.0 A resolution, respectively. Docking simulation between the coupled cytochrome cL molecules and the heterotetrameric methanol dehydrogenase
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purified heme c containing CytcL from Methylophaga aminisulfidivorans (Ma-CytcL), hanging drop vapor diffusion method, mixing of 0.001 ml of 12 mg/ml protein solution containing 800 mM sodium phosphate monobasic, 100 mM HEPES/sodium hydroxide, pH 7.5, with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate monohydrate, 0.1 M bis-Tris, pH 5.5, and 25% PEG 3350, at 20°C for 21 days, X-ray diffraction structure determination analysis at 2.13 A resolution, molecular replacement using the structures of cytochrome cL from Methylobacterium extorquens (Me-CytcL, PDB ID 2C8S) and Hyphomicrobium denitrificans (Hd-CytcL, PDB ID 2D0W) as model structures, modeling
purified native enzyme, hanging drop vapour diffusion method, 8 mg/ml protein in 25 mM Tris-HCl, pH 8.0, mixed with 0.1 M sodium cacodylate pH 6.5, 0.2 M magnesium acetate tetrahydrate and 10% v/v PEG 8000, 20°C, macrocrystals are soaked for 30 s in cryosolution consisting of crystallization solution with 20% v/v glycerol, X-ray diffraction structure determination and analysis at 1.7 A reolution, molecular replacement
purified recombinant MxaJ(residues 12-281), hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M sodium bromide, 20% w/v PEG 3350, and 10% w/v glycerol, at 20°C, X-ray diffraction structure determination and analysis at 1.92 A resolution, modeling
purified enzyme, 5 mg/mL protein in 50 mM Tris-HCl, pH 8.25, and 13.5% PEG 8000, mixed with crystallization solution containing 1 and 50 mM methanol resulting in crystal forms A, B or C with or without incorporated methanol or ethanool, 20°C, X--ray diffraction structure determination and analysis at 1.5-3.0 A resolution, molecular modeling
X-ray diffraction strcuture determination and analysis at 2.6 A resolution, multiple isomorphous replacement, modelling
Ba2+-containing MDH active site model to investigate the two proposed addition-elimination and hydride-transfer methanol oxidation mechanisms
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purified holoenzyme, hanging-drop vapour-diffusion method, 3 ml of 15 mg/ml protein solution, 20 mM Tris buffer, pH 8.0, are placed on siliconized cover slips and mixed with an equal volume of well solution, the cover slip is sealed with high-vacuum grease over a 1 ml well containing 20% PEG 8000, pH 9.0, large crystals after two weeks, X-ray diffraction structure determination and analysis at 1.2 A resolution, modeling
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X-ray diffraction structure determination and analysis at 1.94 A resolution