enzyme binds and degrades heme in a reaction that releases carbon monoxide. Initial intermediates of the reaction of ChuS with hydrogen peroxide, i.e. a ferrous keto pi neutral radical and ferric verdoheme, are in common with heme oxygenases, while a further reaction step, involving the cleavage of the porphyrin ring at adjacent meso-carbons, results in the release of hematinic acid, a tripyrrole product and non-heme iron in the ferric oxidation state
coculture of ChuS-overexpressing Escherichia coli with bone marrow derived macrophages results in decreased IL-12 p40 and increased IL-10 secretion compared to wild-type or ChuS-deficient Escherichia coli. Mice infected with ChuS-overexpressing Escherichia coli have increased levels of hepatic carbon monoxide and decreased serum IL-12 p40
coculture of ChuS-overexpressing Escherichia coli with bone marrow derived macrophages results in decreased IL-12 p40 and increased IL-10 secretion compared to wild-type or ChuS-deficient Escherichia coli. Mice infected with ChuS-overexpressing Escherichia coli have increased levels of hepatic carbon monoxide and decreased serum IL-12 p40
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1.14.14.B10 heme oxygenase (hematinic acid-producing)
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