Journal article
Role of human sulfide: quinone oxidoreductase in H2S metabolism
Methods in enzymology, v 554, pp 255-270
2015
PMID: 25725526
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The first step in the mammalian metabolism of H2S is catalyzed by sulfide:quinone oxidoreductase (SQOR). Human SQOR is an integral membrane protein, which presumably interacts with the inner mitochondrial membrane in a monotopic fashion. The enzyme is a member of a family of flavoprotein disulfide oxidoreductases (e.g., glutathione reductase) that utilize a Cys-S-S-Cys disulfide bridge as an additional redox center. SQOR catalyzes a two-electron oxidation of H2S to sulfane sulfur using coenzyme Q as electron acceptor. The enzyme also requires a third substrate to act as the acceptor of the sulfane sulfur from a cysteine persulfide intermediate. Here, we describe a method for the bacterial expression of human SQOR as a catalytically active membrane-bound protein, procedures for solubilization and purification of the recombinant protein to >95% homogeneity, and spectrophotometric assays to monitor SQOR-mediated H2S oxidation in reactions with different sulfane sulfur acceptors.
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Details
- Title
- Role of human sulfide: quinone oxidoreductase in H2S metabolism
- Creators
- Michael R Jackson - Drexel UniversityScott L Melideo - Drexel UniversityMarilyn Schuman Jorns - Drexel University
- Publication Details
- Methods in enzymology, v 554, pp 255-270
- Publisher
- Elsevier
- Grant note
- R01 GM107389 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; [Retired Faculty]
- Web of Science ID
- WOS:000405617600015
- Scopus ID
- 2-s2.0-84923577868
- Other Identifier
- 991019169130404721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemical Research Methods
- Biochemistry & Molecular Biology