Ferric hemoglobin (metHb) and myoglobin (metMb), present at low levels in vivo, have been
recently found to oxidize hydrogen sulfide (H 2 S) in excess, thus potentially contributing to …

Significance: Along with other gasotransmitters nitric oxide (NO) and carbon monoxide,
hydrogen sulfide (H2S) has recently emerged as an important signaling molecule with a …

Hydrogen sulfide is a cardioprotective signaling molecule but is toxic at elevated
concentrations. Red blood cells can synthesize H 2 S but, lacking organelles, cannot …

Significance: Sulfides are endogenous and ubiquitous signaling species that share the
hemeproteins as biochemical targets with O2, nitric oxide, and carbon monoxide. The …

The mechanism of the metal centered reduction of metmyoglobin (MbFe III) by inorganic
disulfide species has been studied by combined spectroscopic and kinetic analyses, under …

The mechanism of the metal centered reduction of metmyoglobin (MbFeIII) by sulfide
species (H2S/HS–) under an argon atmosphere has been studied by a combination of …

The truncated hemoglobins from Bacillus subtilis (Bs-trHb) and Thermobifida fusca (Tf-trHb)
have been shown to form high-affinity complexes with hydrogen sulfide in their ferric state …

Enzymes in the sulfur network generate the signaling molecule, hydrogen sulfide (H2S),
from the amino acids cysteine and homocysteine. Since it is toxic at elevated concentrations …

Hemoglobin I (HbI) from the clam Lucina pectinata is an intriguing hemeprotein that binds
and transports H2S to sulfide-oxidizing chemoautotrophic bacteria to maintain a symbiotic …

The interactions of the heme iron of hemeproteins with sulfide and disulfide compounds are
of potential interest as physiological signaling processes. While the interaction with …