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Identification of a Stable Flavin-thiolate Adduct in Heterotetrameric Sarcosine Oxidase
Journal article   Open access   Peer reviewed

Identification of a Stable Flavin-thiolate Adduct in Heterotetrameric Sarcosine Oxidase

Robert M.G. Hynson, F. Scott Mathews, Marilyn Schuman Jorns and Marilyn S Jorns
Journal of molecular biology, v 362(4), pp 656-663
2006
PMID: 16934831
url
https://europepmc.org/articles/pmc1635972View
Accepted (AM)Open Access (License Unspecified) Open

Abstract

flavin mononucleotide intramolecular electron transfer oxygen reduction sarcosine oxidation thiolate adduct
Heterotetrameric sarcosine oxidase (TSOX) is a complex bifunctional flavoenzyme that contains two flavins. Most of the FMN in recombinant TSOX is present as a covalent adduct with an endogenous ligand. Enzyme denaturation disrupts the adduct, accompanied by release of a stoichiometric amount of sulfide. Enzyme containing ≥ 90% unmodified FMN is prepared by displacement of the endogenous ligand with sulfite, a less tightly bound competing ligand. Reaction of adduct-depleted TSOX with sodium sulfide produces a stable complex that resembles the endogenous TSOX adduct and known 4a-S-cysteinyl flavin adducts. The results provide definitive evidence for sulfide as the endogenous TSOX ligand and strongly suggest that the modified FMN is a 4a-sulfide adduct. A comparable reaction with sodium sulfide is not detected with other flavoprotein oxidases. A model of the postulated TSOX adduct suggests that it is stabilized by nearby residues that may be important in the electron transferase/oxidase function of the coenzyme.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
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