The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure.
The g-value and linewidth of ESR spectra of methylamine dehydrogenase (primary-amine:(acceptor) oxidoreductase (deaminating) EC 1.4.99.-) and methanol dehydrogenase (alcohol:(acceptor) oxidoreductase, EC 1.1.99.8) are very similar. This similarity is also reflected in electron-nuclear double resonance (ENDOR) results, the coupling constants of two protons in one enzyme equalling those in the other. The presence of a third proton in the ENDOR spectrum of methylamine dehydrogenase suggests a different structure or a different kind of interaction which can be related to the finding that the resolved ROSTHETIC GROUP IS PROTEIN-BOUND. The bound prosthetic group has a high redox-potential, supporting the conclusion from the ESR and ENDOR results that it is a quinone derivative.
D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D008744:Methylamines; D008956:Models, Chemical; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011549:Pseudomonas / Q000201:enzymology*; D011809:Quinones
D005609:Free Radicals; D008744:Methylamines; D011809:Quinones; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors