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The prosthetic group of methylamine dehydrogenase fromPseudomonasAM1:Evidence for a quinone structure

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Protein Structure
0005-2795
Publisher
Elsevier
Publication Date
Volume
622
Issue
2
Identifiers
DOI: 10.1016/0005-2795(80)90050-1
Keywords
  • Methylamine Dehydrogenase
  • Methanol Dehydrogenase
  • Prosthetic Group
  • Quinone Derivative
  • (Esr
  • Endor)
Disciplines
  • Biology

Abstract

Abstract 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 prosthetic 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.

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