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Updated: May 31, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Sulfhydryl oxidases: sources, properties, production and applications
Greta Faccio1, Outi Nivala, Kristiina Kruus
1VTT Technical Research Centre of Finland, PO Box 1000, Espoo 02044 VTT, Finland. greta.faccio@vtt.fi
Sulfhydryl oxidases (SOXs) are enzymes that form disulfide bonds, impacting protein and molecule function. This review summarizes SOX families, production, and applications, highlighting their roles in protein folding and potential uses.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Disulfide bonds are crucial for protein and small molecule functionality.
- Sulfhydryl oxidases (SOXs) catalyze the oxidation of sulfhydryl groups using molecular oxygen.
- SOXs exist intracellularly (protein folding) and extracellularly (small compounds, unknown roles).
Purpose of the Study:
- To provide an up-to-date summary of sulfhydryl oxidases (SOXs).
- To review SOX families, production methods, and current/potential applications.
- To analyze sequence features, domain organization, and physicochemical properties of characterized SOXs.
Main Methods:
- Literature review of scientific publications and patent applications.
- Analysis of sequence features and domain organization.
- Evaluation of physicochemical properties of SOX enzymes.
Main Results:
- SOXs are diverse enzymes with varied substrate specificities and localizations.
- Intracellular SOXs primarily function in protein folding.
- Extracellular SOXs act on small molecules, with physiological roles yet to be elucidated.
- There is a growing body of research and patent activity surrounding SOXs.
Conclusions:
- SOXs represent a significant class of enzymes with diverse biological roles and biotechnological potential.
- Further research into extracellular SOXs may reveal novel physiological functions.
- The increasing number of patents indicates growing industrial interest in SOX applications.
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