Flavoprotein kinetics

W.J.H. van Berkel, J.A.E. Benen, M.H.M. Eppink, M.W. Fraaije

Research output: Chapter in Book/Report/Conference proceedingChapterAcademic

Abstract

Flavoproteins are ubiquitous proteins involved in diverse biological processes ranging from redox catalysis and light emission to DNA repair (1). Based on their function, flavoproteins can be divided into several subclasses including electron transferases, photolyases, synthases, dehydrogenases, disulfide reductases, oxidases, and monooxygenases. Most flavoproteins contain a single flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) molecule as noncovalently bound prosthetic group. Some flavoproteins, like reduced nicotinamide adenine dinucleotide phosphate (NADPH) cytochrome P-450 reductase, contain both FAD and FMN but there are also many flavoproteins that harbor different types of cofactors. Examples of these more “complex” flavoproteins include xanthine oxidase (containing molybdenum and 2Fe−2S centres), trimethylamine dehydrogenase (containing a 4Fe−4S cluster) and flavocytochromes (containing heme).
Original languageEnglish
Title of host publicationMethods in Molecular Biology
Subtitle of host publicationFlavoprotein protocols
EditorsS.K. Chapman, G.A. Reid
Place of PublicationTotowa
PublisherHumana Press
Pages61-85
Volume131
ISBN (Electronic)9781592592661
ISBN (Print)9780896037342
DOIs
Publication statusPublished - 1999

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
Volume131
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

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  • Cite this

    van Berkel, W. J. H., Benen, J. A. E., Eppink, M. H. M., & Fraaije, M. W. (1999). Flavoprotein kinetics. In S. K. Chapman, & G. A. Reid (Eds.), Methods in Molecular Biology: Flavoprotein protocols (Vol. 131, pp. 61-85). (Methods in Molecular Biology; Vol. 131). Humana Press. https://doi.org/10.1385/1-59259-266-X:61