Reaction Mechanism of Heme Oxygenase

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Enzymatic heme degaradation by heme oxygenase, especially its rate-limiting ring opening step, have been studied in detail. Spectroscopic analysis reveals the formation of a ferryl species as a ring opening intermediate. Crystallographic study on an intermediate-enzyme complex combined with theoritical calculations finally elucidate the rate-limiting reaction. We also examined a novel heme cleavage reaction to clarify its mechanism and the new heme catabolites were succesufully detected from cultured mammalian cells.