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Role of human sulfide: quinone oxidoreductase in H2S metabolism
Journal article   Peer reviewed

Role of human sulfide: quinone oxidoreductase in H2S metabolism

Michael R Jackson, Scott L Melideo and Marilyn Schuman Jorns
Methods in enzymology, v 554, pp 255-270
2015
PMID: 25725526

Abstract

Biocatalysis Enzyme Assays Escherichia coli Humans Hydrogen Sulfide - chemistry Hydrogen Sulfide - metabolism Kinetics Oxidation-Reduction Quinone Reductases - chemistry Quinone Reductases - isolation & purification Quinone Reductases - physiology
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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Web of Science research areas
Biochemical Research Methods
Biochemistry & Molecular Biology
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