Chemistry of flavoenzymes

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

Abstract

Flavoenzymes are omnipresent in nature and are involved in many cellular processes. Flavoenzymes typically contain the vitamin B2 derivatives FAD and FMN as a redox-active prosthetic group. By varying the protein environment around the isoalloxazine ring of the flavin, evolution has created a great diversity of flavoprotein active sites and catalytic machineries. Most flavoenzymes perform one- or two-electron redox reactions and belong to the following groups: Flavoprotein reductases primarily use NAD(P)H as electron donor and pass these electrons to a protein substrate or another electron acceptor. Flavoprotein dehydrogenases oxidize organic substrates and mainly use quinones and electron transfer proteins as electron acceptors. Flavoprotein disulfide oxidoreductases contain active-site thiols. They use a dithiol substrate and NAD+ to form a disulfide product and NADH or act in the other direction yielding NAD(P)+ and a reduced (dithiol) product. Some flavoprotein (di)thiol oxidoreductases stabilize a reactive and reversibly oxidized cysteine in their active site. Flavoprotein oxidases catalyze the conversion of a substrate single bond to a double bond. The reduced flavin generated during this reaction is reoxidized by molecular oxygen to form hydrogen peroxide. Flavoprotein monooxygenases mainly use NAD(P)H as an electron donor and insert one atom of molecular oxygen into their substrates. By doing so, they act in different biological processes, ranging from lignin degradation and detoxification to the biosynthesis of polyketides and plant hormones.
LanguageEnglish
Title of host publicationWiley Encyclopedia of Chemical Biology
EditorsT. Begley
Place of Publication[S.l.]
PublisherJohn Wiley and Sons
DOIs
Publication statusPublished - 2008

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Flavoproteins
NAD
Electrons
Oxidoreductases
Substrates
Molecular oxygen
Sulfhydryl Compounds
Disulfides
Polyketides
Flavin Mononucleotide
Quinones
Detoxification
Proteins
Flavin-Adenine Dinucleotide
Plant Growth Regulators
Riboflavin
Lignin
Redox reactions
Biosynthesis
Mixed Function Oxygenases

Cite this

van Berkel, W. J. H. (2008). Chemistry of flavoenzymes. In T. Begley (Ed.), Wiley Encyclopedia of Chemical Biology [S.l.]: John Wiley and Sons. https://doi.org/10.1002/9780470048672.wecb168
van Berkel, W.J.H. / Chemistry of flavoenzymes. Wiley Encyclopedia of Chemical Biology. editor / T. Begley. [S.l.] : John Wiley and Sons, 2008.
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abstract = "Flavoenzymes are omnipresent in nature and are involved in many cellular processes. Flavoenzymes typically contain the vitamin B2 derivatives FAD and FMN as a redox-active prosthetic group. By varying the protein environment around the isoalloxazine ring of the flavin, evolution has created a great diversity of flavoprotein active sites and catalytic machineries. Most flavoenzymes perform one- or two-electron redox reactions and belong to the following groups: Flavoprotein reductases primarily use NAD(P)H as electron donor and pass these electrons to a protein substrate or another electron acceptor. Flavoprotein dehydrogenases oxidize organic substrates and mainly use quinones and electron transfer proteins as electron acceptors. Flavoprotein disulfide oxidoreductases contain active-site thiols. They use a dithiol substrate and NAD+ to form a disulfide product and NADH or act in the other direction yielding NAD(P)+ and a reduced (dithiol) product. Some flavoprotein (di)thiol oxidoreductases stabilize a reactive and reversibly oxidized cysteine in their active site. Flavoprotein oxidases catalyze the conversion of a substrate single bond to a double bond. The reduced flavin generated during this reaction is reoxidized by molecular oxygen to form hydrogen peroxide. Flavoprotein monooxygenases mainly use NAD(P)H as an electron donor and insert one atom of molecular oxygen into their substrates. By doing so, they act in different biological processes, ranging from lignin degradation and detoxification to the biosynthesis of polyketides and plant hormones.",
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van Berkel, WJH 2008, Chemistry of flavoenzymes. in T Begley (ed.), Wiley Encyclopedia of Chemical Biology. John Wiley and Sons, [S.l.]. https://doi.org/10.1002/9780470048672.wecb168

Chemistry of flavoenzymes. / van Berkel, W.J.H.

Wiley Encyclopedia of Chemical Biology. ed. / T. Begley. [S.l.] : John Wiley and Sons, 2008.

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

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AB - Flavoenzymes are omnipresent in nature and are involved in many cellular processes. Flavoenzymes typically contain the vitamin B2 derivatives FAD and FMN as a redox-active prosthetic group. By varying the protein environment around the isoalloxazine ring of the flavin, evolution has created a great diversity of flavoprotein active sites and catalytic machineries. Most flavoenzymes perform one- or two-electron redox reactions and belong to the following groups: Flavoprotein reductases primarily use NAD(P)H as electron donor and pass these electrons to a protein substrate or another electron acceptor. Flavoprotein dehydrogenases oxidize organic substrates and mainly use quinones and electron transfer proteins as electron acceptors. Flavoprotein disulfide oxidoreductases contain active-site thiols. They use a dithiol substrate and NAD+ to form a disulfide product and NADH or act in the other direction yielding NAD(P)+ and a reduced (dithiol) product. Some flavoprotein (di)thiol oxidoreductases stabilize a reactive and reversibly oxidized cysteine in their active site. Flavoprotein oxidases catalyze the conversion of a substrate single bond to a double bond. The reduced flavin generated during this reaction is reoxidized by molecular oxygen to form hydrogen peroxide. Flavoprotein monooxygenases mainly use NAD(P)H as an electron donor and insert one atom of molecular oxygen into their substrates. By doing so, they act in different biological processes, ranging from lignin degradation and detoxification to the biosynthesis of polyketides and plant hormones.

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van Berkel WJH. Chemistry of flavoenzymes. In Begley T, editor, Wiley Encyclopedia of Chemical Biology. [S.l.]: John Wiley and Sons. 2008 https://doi.org/10.1002/9780470048672.wecb168