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- W2083431904 abstract "Historically, hydrogen sulfide (H(2)S) has been regarded as a poisonous gas, with a wide spectrum of toxic effects. However, like ·NO and CO, H(2)S is now referred to as a signaling gas involved in numerous physiological processes. The list of reports highlighting the physiological effects of H(2)S is rapidly expanding and several drug candidates are now being developed. As with ·NO and CO, not a single H(2)S target responsible for all the biological effects has been found till now. Nevertheless, it has been suggested that H(2)S can bind to hemeproteins, inducing different responses that can mediate its effects. For instance, the interaction of H(2)S with cytochrome c oxidase has been associated with the activation of the ATP-sensitive potassium channels, regulating muscle relaxation. Inhibition of cytochrome c oxidase by H(2)S has also been related to inducing a hibernation-like state. Although H(2)S might induce these effects by interacting with hemeproteins, the mechanisms underlying these interactions are obscure. Therefore, in this review we discuss the current state of knowledge about the interaction of H(2)S with vertebrate and invertebrate hemeproteins and postulate a generalized mechanism. Our goal is to stimulate further research aimed at evaluating plausible mechanisms that explain H(2)S reactivity with hemeproteins." @default.
- W2083431904 created "2016-06-24" @default.
- W2083431904 creator A5064410183 @default.
- W2083431904 creator A5081724069 @default.
- W2083431904 creator A5087924494 @default.
- W2083431904 date "2011-07-15" @default.
- W2083431904 modified "2023-10-15" @default.
- W2083431904 title "Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries" @default.
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- W2083431904 doi "https://doi.org/10.1089/ars.2010.3698" @default.
- W2083431904 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3118656" @default.
- W2083431904 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21050142" @default.
- W2083431904 hasPublicationYear "2011" @default.
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