Hydrogen Sulfide Oxidation by Sulfide Quinone Oxidoreductase.
Hydrogen Sulfide Oxidation by Sulfide Quinone Oxidoreductase.
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DOI:
10.1002/cbic.202000661
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发表时间:
2021-03-16
期刊:
影响因子:
--
通讯作者:
Banerjee R
中科院分区:
文献类型:
--
作者:
Landry AP;Ballou DP;Banerjee R
Hydrogen sulfide (H2S) is an environmental toxin and a heritage of ancient microbial metabolism, which has stimulated new interest following its discovery as a neuromodulator. While many physiological responses have been attributed to low H2S levels, higher levels inhibit complex IV in the electron transport chain. To prevent respiratory poisoning, a dedicated set of enzymes comprising the mitochondrial sulfide oxidation pathway exists to clear H2S. The committed step in this pathway is catalyzed by sulfide quinone oxidoreductase (SQOR), which couples sulfide oxidation to coenzyme Q10 reduction in the electron transport chain. The SQOR reaction prevents H2S accumulation and generates highly reactive persulfide species as products, which can be further oxidized or can modify cysteine residues in proteins via persulfidation. Here, we review the kinetic, and structural characteristics of human SQOR, and how its unconventional redox cofactor configuration and substrate promiscuity lead to sulfide clearance and potentially expand the signaling potential of H2S. This dual role of SQOR makes it a promising target for H2S-based therapeutics. Regulating sulfide toxicity and signaling: Utilizing an active site cysteine trisulfide, human sulfide quinone oxidoreductase detoxifies hydrogen sulfide, a respiratory poison. Herein, we detail the remarkable enzymology of sulfide quinone oxidoreductase and its potential modulation of sulfide signaling.
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发表时间:
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