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).
|Title of host publication||Methods in Molecular Biology|
|Subtitle of host publication||Flavoprotein protocols|
|Editors||S.K. Chapman, G.A. Reid|
|Place of Publication||Totowa|
|Publication status||Published - 1999|
|Name||Methods in Molecular Biology|
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