Spectral properties of the higher oxidation states of prostaglandin H synthase.
Spectral properties of the higher oxidation states of prostaglandin H synthase.
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DOI：
10.1016/s0021-9258(18)95676-0
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发表时间：
1985-12
期刊：
影响因子：
--
通讯作者：
A. Lambeir;C. Markey;H. Dunford;L. Marnett
中科院分区：
文献类型：
--
作者：
A. Lambeir;C. Markey;H. Dunford;L. Marnett
前列腺素H（PGH）合酶与有机氢过氧化物和脂肪酸氢过氧化物在毫秒时间尺度上反应，以产生光谱上类似于辣根过氧化物酶的化合物I的中间体。PGH合酶的化合物I在170 ms内转化为化合物II。化合物II在几秒钟内衰变为静息酶。因此，PGH合酶的过氧化物酶反应似乎涉及天然酶、化合物I和化合物II的循环，这是典型的含血红素的过氧化物酶。化合物I的Soret吸收最大值似乎出现在412 nm处，但可能存在少量化合物II。化合物II、亚铁酶和含氧亚铁酶（化合物III）的Soret最大值分别出现在420、433和419处。PGH合酶与花生四烯酸反应的快速扫描分析揭示了化合物II的吸光度，但没有亚铁或氧亚铁酶的证据。
Prostaglandin H (PGH) synthase reacts with organic hydroperoxides and fatty acid hydroperoxides on a millisecond time scale to generate an intermediate that is spectrally similar to compound I of horseradish peroxidase. Compound I of PGH synthase is converted to compound II within 170 ms. Compound II decays to resting enzyme in a few seconds. Thus, the peroxidase reaction of PGH synthase appears to involve a cycle of native enzyme, compound I, and compound II, typical of heme-containing peroxidases. The Soret absorption maximum of compound I appears to occur at 412 nm but a small amount of compound II may be present. Soret maxima occur at 420, 433, and 419 for compound II, the ferrous enzyme, and the oxyferrous enzyme (compound III), respectively. Rapid scan analysis of the reaction of PGH synthase with arachidonic acid reveals the absorbance of compound II but no evidence for ferrous or oxyferrous enzyme.