Abstract
Flavoproteins are involved in a variety of biological electron transfer processes, from energy accumulation in respiratory and photosynthetic electron transfer chains to oxidation of toxic compounds by cytochrome P450-dependent systems. The structure and function of free and protein bound flavins have been a subject of extensive studies. This effort has resulted in our current understanding of the chemistry and significance of flavins in living cells, as summarized in a number of reviews (1–4).
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Edmondson, D. E. (1978) ESR of free radicals in enzyme systems, in Biological Magnetic Resonance, vol. 1 (Berliner, L. J. and Reuben, J., eds.), Plenum, New York, pp. 205–237.
Müller, F. (1983) The flavin redox-system and its biological function. in: Topics in Current Chemistry, vol. 108, Radicals in Biochemistry, Springer Verlag, New York, pp. 71–107.
Edmondson, D. E. and Tollin, G. (1983) Semiquinone formation in flavo-and metalloflavoproteins, in Topics in Current Chemistry, vol. 108, Springer Verlag, New York, pp. 109–138.
Ghisla, S. and Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181, 1–17.
von Dudley, K. H., Eriksson, L. E. G., and Ehrenberg, A., and Müller, F. (1964) Spektren und strukturen der am flavin-redoxsystem beteiligten partikeln. Helv. Chim. Acta 47, 1354–1383.
Eriksson, L. E. G. and Ehrenberg, A. (1964) Electron spin resonance study on anionic flavin free radical. Acta Chem. Scand. 18, 1437–1453.
Ehrenberg, A., Müller, F., and Hemmerich, P. (1967) Basicity, visible spectra, and electron spin resonance of flavosemiquinone anions. Eur. J. Biochem. 2, 286–293.
Müller, F., Hemmerich, P., Ehrenberg, A., Palmer, G., and Massey, V. (1970) The chemical and electronic structure of the neutral flavin radical as revealed by electron spin resonance spectroscopy of chemically and isotopically substituted derivatives. Eur. J. Biochem. 14, 185–196.
Müller, F., Hemmerich, P., and Ehrenberg, A. (1969) On the molecular and submolecular structure of flavin free radicals and their properties, in Flavin and Flavoproteins (Kamin, H., ed.), University Park Press, Baltimore, MD, pp. 107–122.
Müller, F., Brüstlein, M., Hemmerich, P., Massey, V., and Walker, W. H. (1972) Light-absorption studies on neutral flavin radicals. Eur. J. Biochem. 25, 573–580.
Massey, V. and Palmer, G. (1966) On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry 5, 3181–3189.
Lostao, A., Gomez-Moreno, C., Mayhew, S. G., and Sancho, J. (1997) Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials. Biochemistry 36, 14,334–13,344.
Massey, V., Palmer, G., Williams, C. H., Swoboda, B. E. P., and Sands, R. H. (1966) Flavin semiquinones and flavoprotein catalysis, in Flavin and Flavoproteins (Slater, E. C., ed.), Elsevier, New York, pp. 133–158.
Kosower, E. M. (1966) The role of charge-transfer complexes in flavin chemistry and biochemistry, in Flavin and Flavoproteins (Slater, E. C. ed.), Elsevier, New York, pp. 1–14.
Carrington, A. and McLachlan, A. D. (1967) Introduction to magnetic resonance. Harper and Row Publishing, New York.
Hyde, J. S. (1974) Paramagnetic relaxation. Ann. Rev. Phys. Chem. 25, 407–435.
Ingram, D. J. E. (1969) Biological and Biochemical Applications of Electron Spin Resonance, Plenum, New York.
Hoff, A. J., ed. (1989) Advanced EPR, in Application in Biology and Biochemistry, Elsevier, New York.
Palmer, G., Müller, F., and Massey, V. (1969) Electron paramagnetic resonance studies of flavoprotein radicals, in Flavins and Flavoproteins (Kamin, H., ed.), Elsevier, New York, pp. 123–140.
Murataliev, M. B., Klein, M., Fulco, A., and Feyereisen, R. (1997) Functional interactions in cytochrome P450BM3. Flavin semiquinone intermediates, role of NADP(H), and mechanism of electron transfer by the flavoprotein domain. Biochemistry 36, 8401–8412.
Hyde, J. S., Eriksson, L. E. G., and Ehrenberg, A. (1970) EPR relaxation of slowly moving flavin radicals: “anomalous” saturation. Biochim Biophys. Acta. 222, 688–692.
Hyde, J. S. (1967) Electron nuclear double resonance using an intense nuclear radio frequency field, in Magentic Resonance in Biological Systems, Pergamon Press, Oxford, UK, pp. 63–84.
Norris, J. R., Thurnauer, M. C., and Bowman, M. K. (1980) Electron spin echo spectroscopy and the study of biological structure and function. Adv. Biol. Med. Phys. 17, 365–416.
Iyanagi, T. (1977) Redox properties of microsomal reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5. Biochemistry 16, 2725–2730.
Nonaka, Y., Fujii, S., and Yamano, T. (1986) The semiquinone state of NADPH-adrenodoxin oxidoreductase in the course of anerobic reduction with NADPH. J. Biochem. 99, 803–814.
Peterson, J. A. and Boddupalli, S. S. (1992) P450BM-3: reduction by NADPH and sodium dithionite. Arch. Biochem. Biophys. 294, 654–661.
Daff, S. N., Chapman, S. K., Turner, K. L., Holt, R. A., Govindaraj, S., Poulos, T. L., and Munro, A. W. (1997) Redox control of the catalytic cycle of flavo-cytochrome P-450 BM3. Biochemistry 36, 13,816–13,823.
DeRose, V. J., Woo, J. C. G., Hawe, W. P., Hoffman, B. M., Silverman, R. B., and Yelekci, K. (1996) Observation of a flavin semiquinonein the resting state of monoamine oxidase B by electron paramagnetic resonance and electron nuclear double resonance spectroscopy. Biochemistry 35, 11,085–11,091.
Lambeth, J. D. and Kamin, H. (1976) Adrenodoxin reductase. Properties of the complexes of reduced enzyme with NADP+ and NADPH. J. Biol. Chem. 251, 4299–4306.
Narhi, L. O. and Fulco, A. J. (1986) Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monoxygenase induced by barbiturates in Bacillus megaterium. J. Biol. Chem. 261, 7160–7169.
Narhi, L. O. and Fulco, A. J. (1987) Identification and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium. J. Biol. Chem. 262, 6683–6690.
Masters, B. S. S., Kamin, H., Gibson, Q. H., and Williams, C. H., Jr. (1965) Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 240, 921–931.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Humana Press Inc., Totowa, NJ
About this protocol
Cite this protocol
Murataliev, M.B. (1999). Application of Electron Spin Resonance (ESR) for Detection and Characterization of Flavoprotein Semiquinones. In: Chapman, S.K., Reid, G.A. (eds) Flavoprotein Protocols. Methods in Molecular Biology, vol 131. Humana Press. https://doi.org/10.1385/1-59259-266-X:97
Download citation
DOI: https://doi.org/10.1385/1-59259-266-X:97
Publisher Name: Humana Press
Print ISBN: 978-0-89603-734-2
Online ISBN: 978-1-59259-266-1
eBook Packages: Springer Protocols