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Structure of the Modified Heme in Allylbenzene-Inactivated Chloroperoxidase Determined by Q-Band CW and Pulsed ENDOR

机译:Q波段连续波和脉冲ENDOR法测定烯丙基苯灭活的氯过氧化物酶中修饰血红素的结构

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摘要

During the epoxidation of allylbenzene, chloroperoxidase (CPO) is converted to an inactive green species in which the prosthetic heme has been modified by addition of the alkene puls an oxygen atom (Dexter, A.F.; Hager, L.P.J.Am.Chem. Soc.1995, 117,817-818). We have used Q-band continuous wave and pulsed electron- nuclear double resonance (ENDOR) spectroscopy to study the CPO heme in situ following inactivation with allylbenzene, using samples prepared in natural isotopic abundance, with ~15N-labeled enzyme, and with allylbenzene labeled with ~2H or ~13C in specific vinylic positions.
机译:在烯丙基苯的环氧化过程中,氯过氧化物酶(CPO)转化为非活性绿色物质,其中通过添加烯烃脉冲和氧原子对人工血红素进行了修饰(Dexter,AF; Hager,LPJAm.Chem。Soc.1995, 117,817-818)。我们已经使用Q波段连续波和脉冲电子核双共振(ENDOR)光谱研究了烯丙基苯失活,天然同位素丰度制备的样品,〜15N标记的酶和烯丙基苯标记的灭活后的CPO血红素原位。在特定的乙烯基位置带有〜2H或〜13C。

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