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Investigations of two-component flavin-dependent monooxygenase systems.

Authors
  • Robbins, John M1
  • Ellis, Holly R2
  • 1 School of Chemical & Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, United States. , (Georgia)
  • 2 Department of Chemistry and Biochemistry, Auburn University, Auburn, AL, United States. Electronic address: [email protected] , (United States)
Type
Published Article
Journal
Methods in enzymology
Publication Date
Jan 01, 2019
Volume
620
Pages
399–422
Identifiers
DOI: 10.1016/bs.mie.2019.03.018
PMID: 31072495
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Bacterial two-component flavin-dependent monooxygenase systems catalyze the oxidation of diverse metabolic reactions. There are several shared mechanistic features in the two-component monooxygenase systems that differ from canonical monooxygenase enzymes. The flavin reductases catalyze the reductive half-reaction, and the reduced flavin is transferred to the monooxygenase enzyme. The oxidative half-reaction catalyzed by the monooxygenase enzyme has been proposed to occur through the formation of a (hydro)peroxyflavin intermediate. In some two-component flavin-dependent systems the mechanism of flavin transfer involves protein-protein interactions between the flavin reductase and monooxygenase enzyme. Methods are presented that provide an alternative approach from flavin-bound monooxygenases to evaluate the kinetic properties and flavin transfer mechanism of the two-component flavin-dependent monooxygenase systems. © 2019 Elsevier Inc. All rights reserved.

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