The interaction of methanol dehydrogenase and its cytochrome electron acceptor.
A fluorescence method is described for direct measurement of the interaction between methanol dehydrogenase (MDH) and its electron acceptor cytochrome cL. This has permitted a distinction to be made between factors affecting electron transfer and those affecting the initial binding or docking process. It was confirmed that the initial interaction is electrostatic, but previous conclusions with respect to the mechanism of EDTA inhibition have been modified. It is proposed that the initial 'docking' of MDH and cytochrome cL is by way of ionic interactions between lysyl residues on its surface and carboxylate groups on the surface of cytochrome cL. This interaction is not inhibited by EDTA, which we suggest acts by binding to nearby lysyl residues, thus preventing movement of the 'docked' cytochrome to its optimal position for electron transfer, which probably involves interaction with the hydrophobic funnel in the surface of MDH.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004579:Electron Transport; D008772:Methylococcaceae / Q000201:enzymology*; D009994:Osmolar Concentration; D011485:Protein Binding; D012965:Sodium Chloride / Q000494:pharmacology; D013050:Spectrometry, Fluorescence; D014462:Ultrafiltration / Q000379:methods
D003574:Cytochrome c Group; D012965:Sodium Chloride; C058498:cytochrome C(L); D004492:Edetic Acid; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor)