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Inside the lesion, hemoglobin (Hb) is oxidized to ferri\u2010 and ferrylHb which exhibit prooxidant and proinflammatory activities. Cystathione gamma\u2010lyase\u2010 (CSE\u2010) derived H<jats:sub>2<\/jats:sub>S has been suggested to possess various antiatherogenic actions. Expression of CSE was upregulated predominantly in macrophages, foam cells, and myofibroblasts of human atherosclerotic lesions derived from carotid artery specimens of patients. A similar pattern was observed in aortic lesions of apolipoprotein E\u2010deficient mice on high\u2010fat diet. We identified several triggers for inducing CSE expression in macrophages and vascular smooth muscle cells including heme, ferrylHb, plaque lipids, oxidized low\u2010density lipoprotein, tumor necrosis factor\u2010<jats:italic>\u03b1<\/jats:italic>, and interleukin\u20101<jats:italic>\u03b2<\/jats:italic>. In the interplay between hemoglobin and atheroma lipids, H<jats:sub>2<\/jats:sub>S significantly mitigated oxidation of Hb preventing the formation of ferrylHb derivatives, therefore providing a novel function as a heme\u2010redox\u2010intermediate\u2010scavenging antioxidant. By inhibiting Hb\u2010lipid interactions, sulfide lowered oxidized Hb\u2010mediated induction of adhesion molecules in endothelium and disruption of endothelial integrity. Exogenous H<jats:sub>2<\/jats:sub>S inhibited heme and Hb\u2010mediated lipid oxidation of human atheroma\u2010derived lipid and human complicated lesion. 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