Reactome | SQR oxidizes sulfide to bound persulfide

SQR oxidizes sulfide to bound persulfide

Stable Identifier

R-HSA-1614665

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial inner membrane, cytosol

ReviewStatus

5/5

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SQR oxidizes sulfide to bound persulfide

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When SQR is in the oxidized state, it can bind hydrogen sulfide as persulfide to one of its own cysteine residue, the electrons being transferred to ubiquinone. After that the additional sulfur is dioxygenated by another enzyme (ETHE1). The activity of human SQR was deduced from the orthologue in Arenicola marina (Theissen et al. 2003, Hildebrandt & Grieshaber 2008).

Literature References

PubMed ID	Title	Journal	Year
18494801	Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria Hildebrandt, TM, Grieshaber, MK	FEBS J	2008
12832624	Single eubacterial origin of eukaryotic sulfide:quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times Theissen, U, Hoffmeister, M, Grieshaber, M, Martin, W	Mol Biol Evol	2003

Participants

Input

Output

Participates

as an event of

Sulfide oxidation to sulfate (Homo sapiens)

Catalyst Activity

sulfide:quinone oxidoreductase activity of SQR:FAD [mitochondrial inner membrane]

Physical Entity

SQR:FAD [mitochondrial inner membrane] (Homo sapiens)

Activity

sulfide:quinone oxidoreductase activity (GO:0070224)

Inferred From

Sqr oxidizes sulfide to bound persulfide (Arenicola marina)

Authored

Stephan, R (2010-10-24)

Reviewed

D'Eustachio, P (2011-10-13)

Created

Jassal, B (2011-09-29)

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