ESR and ENDOR at 9 and 35 GHz on a powder of the enzyme methanol dehydrogenase from Hyphomicrobium X

Journal Article · Tue May 15 04:00:00 EDT 1979 · J. Chem. Phys.; (United States)

DOI:https://doi.org/10.1063/1.437286· OSTI ID:6083651

de Beer, R; van Ormondt, D; van Ast, M A; Banen, R; Duine, J A; Frank, J

ESR and ENDOR at 9 and 35 GHz have been applied to a powder of the enzyme methanol dehydrogenase from Hyphomicrobium X. The observed g-tensor and ESR linewidth suggest that the protein-bonded free radical originates from a quinone. ENDOR measurements at 35 GHz show that there are two strongly coupled protons in the free radical. The ENDOR response of the proton with the largest hyperfine coupling has been simulated by means of a line shape model. From this simulation the principal values of the hyperfine tensor could be extracted. The derived values indicate that the proton concerned is attached directly to a carbon of the quinoid ring.

• Research Organization: Department of Physics, Technische Hogeschool Delft, P.O. Box 5046, 2600 GA Delft, The Netherlands
• OSTI ID: 6083651
• Journal Information: J. Chem. Phys.; (United States), Journal Name: J. Chem. Phys.; (United States) Vol. 70:10; ISSN JCPSA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALCOHOLS
DEHYDROGENASES
ELECTRON SPIN RESONANCE
ENDOR
ENZYMES
HYDROXY COMPOUNDS
MAGNETIC RESONANCE
METHANOL
ORGANIC COMPOUNDS
OXIDOREDUCTASES
RADICALS
RESONANCE
TENSORS