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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Enhanced production of ethylene from methional by iron chelates and heme containing proteins in the system consisting of quinone compounds and NADPH-cytochrome P-450 reductase.

The addition of iron chelates or heme containing proteins to the systems consisting of NADPH-cytochrome P-450 reductase and quinone compounds, such as vitamin K3 (menadione), adriamycin, tetrahydropyranyladriamycin, daunomycin, aclacinomycin A, carbazilquinone, and mitomycin C, showed the enhanced production of ethylene from methional. In the vitamin K3 system, the effective iron chlates were Fe(II)-EDTA, Fe(II)-ADP, Fe(II)-bleomycin A2, and hemin, and the effective iron containing proteins were methemoglobin, myoglobin, ferredoxin, and partially purified cytochromes P-450, P-420, and b5, and the reversed effects were observed by horse radish peroxidase and sulfite reductase from yeast. In the system consisting of aclacinomycin A and methemoglobin, the ethylene production was potently inhibited by radical scavengers, such as Tiron, Tris, thiourea, and KI, and weakly inhibited by some other scavengers. In the system containing vitamin K3 and methemoglobin, the ethylene production was potently inhibited by catalase, but partially by superoxide dismutase, KCN, and NaN3. In this system, the absorption spectrum of methemoglobin was immediately changed to oxyform and quenched with time, and catalase protected the decrement of the spectrum. The addition of hydrogen peroxide or cumene hydroperoxide to methemoglobin also produced ethylene from methional.[1]


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