… the ability of ferric hemoglobin to oxidize sulfide to thiosulfate and iron-… myoglobin exhibits
a similar capacity for sulfide oxidation. We have trapped and characterized iron-bound sulfur …

… 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 …

… as a canonical hydrogen sulfide oxidation pathway. In this … between hydrogen sulfide and
hemoglobin, myoglobin and … Hydrogen sulfide oxidation by ferric hemoglobin, myoglobin …

… initiate protein cross-linking, was found to be reduced by hydrogen sulfide to yield sulfmyoglobin.
Horse heart myoglobin, void of cysteine, was used to avoid possible interference from …

… Nitric oxide (NO), carbon monoxide (CO) and hydrogen sulfide (H 2 S) are all endogenously
generated species with important physiological functions [eg, Ref. [[1], [2], [3]]]. Due to their …

… of ferryl myoglobin formation and its oxidative effects on low density lipoproteins by nitric
oxideFEBS … The modulation of ferryl myoglobin formation and its oxidative effects on low density …

… The modification of human myoglobin (HMb) by reaction with nitrite and hydrogen peroxide
… H 2 O 2 are formed in vivo under conditions of oxidative and nitrative stress, where protein …

… After complete reduction of the oxoferryl form of myoglobin the … myoglobin (Table 2). This
means that TDS is the main product of thiamine oxidation, and the oxoferryl form of myoglobin …

… The conversion of myoglobin to sulfmyoglobin resulted from the production of H2S by bacteria
tentatively identified as Pseudomonas mephitica. This organism produced H2S only when …

… of H 2 S, long term adaptations of chronic H 2 S presence or absence, both in skeletal
muscle metabolism, and in overall physical capacity such as hemoglobin and myoglobin levels, …