Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Abstract

Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (•NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins. For example, interaction of H2S with the oxygenated form of human hemoglobin and myoglobin produces a sulfheme protein complex that has been implicated in H2S degradation. The presence of this sulfheme derivative has also been used as a marker for endogenous H2S synthesis and metabolism. Remarkably, human catalases and peroxidases also generate this sulfheme product. In this review, we describe the structural and functional aspects of the sulfheme derivative in these proteins and postulate a generalized mechanism for sulfheme protein formation. We also evaluate the possible physiological function of this complex and highlight the issues that remain to be assessed to determine the role of sulheme proteins in H2S metabolism, detection and physiology.

Upregulation and Mitochondrial Sequestration of Hemoglobin Occur in Circulating Leukocytes during Critical Illness, Conferring a Cytoprotective Phenotype

“…Similarly, with respect to the interactions of Hbs with oxyradicals, substantial work has been conducted already, which can be reviewed in the literature (37)(38)(39). With respect to the interactions of Hbs with H 2 S, several lines of studies have demonstrated the formation of sulfhemoglobins (40,41), and Banerjee and colleagues have recently outlined several novel aspects of the interaction, especially with respect to the interactions of H 2 S with methemoglobin (42).…”

Persulfidation (S-sulfhydration) and H2S

“…In fact H 2 S shows biphasic effects on whole cell respiration, stimulating it at low doses and then completely inhibiting it at higher concentrations (Koenitzer et al 2007). Binding of H 2 S to haem has an important function in mollusc, Lucina pectinata, where H 2 S binds to haemoglobin I and is then transported to the symbiotic chemoautotrophic bacteria living in their gills (Ríos-González et al 2014). …”

Effect of green tea on interaction of lipid oxidation products with sarcoplasmic and myofibrillar protein homogenates extracted from bovine top round muscle

“…4). This decrease may have occurred because of the oxidation of Mb in SP (Ríos-González, Román-Morales, Pietri, & López-Garriga, 2014;Romero, Ordonez, Arduini, & Cadenas, 1992) or most likely because the amino acids develop covalent bonds with green tea quinones formed by the oxidation of phenols, producing thiol-quinone adducts (Jongberg et al 2011). …”