Hydrogen sulfide (H 2 S) has been traditionally considered to be a toxic molecule for
mammals. However, it can be formed endogenously and exert physiological effects with …

Hydrogen sulfide (H2S/HS–) can be formed in mammalian tissues and exert physiological
effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) …

The chemistry of hydrogen sulfide (H2S) has been directed towards physiologically relevant
hemeproteins, including myoglobin, hemoglobin, and other similar proteins. Despite …

Hydropersulfides are reported to be good biological reductants, superior to thiols and akin to
selenols. As such, they have been previously shown to reduce metalloproteins such as ferric …

Sulfhemoglobinemia is an incurable disease caused by an overdose of sulfur-containing
drugs with oxidizing properties. Its diagnosis remains hindered due to the similarity of …

Sulfite reductase (SiR) contains in the active site a unique assembly of siroheme and a
[4Fe4S] cluster, linked by a cysteine residue. Siroheme is a doubly reduced variant of heme …

Since the 1863 discovery of a new green hemoglobin derivative called “sulfhemoglobin”, the
nature of the characteristic 618 nm absorption band has been the subject of several …

The present study reports findings regarding the contrast between H 2 S interaction with
bovine hemoglobin (Hb) and horse heart myoglobin (Mb), in terms of binding and …

Hemoglobin in its ferryl form oxidizes hydrogen sulfide and is transformed to
sulfhemoglobin, where the sulfur is inserted covalently at the heme edge. Shown here is …

The biological chemistry of hydrogen sulfide (H 2 S) with physiologically important heme
proteins is in the focus of redox biology research. In this study, we investigated the …