A nuclear Overhauser effect study of the heme crevice in the resting state and compound I of horseradish peroxidase: evidence for cation radical delocalization to the proximal histidine.
A nuclear Overhauser effect study of the heme crevice in the resting state and compound I of horseradish peroxidase: evidence for cation radical delocalization to the proximal histidine.
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静息状态下血红素缝隙和辣根过氧化物酶化合物 I 的核奥沃豪瑟效应研究：阳离子自由基离域至近端组氨酸的证据。
DOI：
10.1021/bi00415a003
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发表时间：
1988
期刊：
影响因子：
2.9
通讯作者：
deRopp,JS
中科院分区：
文献类型：
--
作者：
Thanabal,V;LaMar,GN;deRopp,JS
加州大学戴维斯分校化学系和UCD NMR设备，95616收到1988年1月27日；修订稿收到1988年3月24日摘要：利用核Overhauser效应(NOE)从每个物种中已知的亚铁血红素甲基分配开始，对高自旋休止态辣根过氧化物酶(HRP)及其双氧化反应形式化合物I(HRP-I)的超精细位移共振进行了指认。尽管存在有效的自旋晶格驰豫和非常广泛的共振，但所有相邻的吡咯取代基都观察到了显著的NOE，这使得难以捉摸的丙酸α-亚甲基质子得以归属。在静息状态下，这直接导致近端的His-170H^峰的身份。确定HRP-I中最强的接触位移单质子共振不是由卟啉引起的，这意味着阳离子自由基必须离域到一些氨基酸残基上。HRP-I中非血红素接触位移信号的驰豫特性支持将这一贡献残基识别为近端的His-170。对接触位移模式和NOE变化的详细分析表明，化合物I的形成伴随着6-丙酸基的~5个旋转。讨论了在相关细胞色素c过氧化物酶的化合物I中，近端组氨酸离域的卟啉阳离子自由基对单一氨基酸中心自由基位置的影响。
Department of Chemistry and UCD NMRFacility, University of California, Davis, California 95616 Received January 27, 1988; Revised Manuscript Received March 24, 1988 abstract: The assignment of resolved hyperfine-shifted resonances in high-spin resting state horseradish peroxidase (HRP) and its double-oxidized reactive form, compound I (HRP-I), has been carried out by using the nuclear Overhauser effect (NOE) starting with the known heme methyl assignments in each species. In spite of the efficient spin-lattice relaxation and very broad resonances, significant NOEs were observed for all neighboring pyrrole substituents, which allowed the assignment of the elusive propionate a-methylene protons. In the resting state HRP, this leads directly to the identity of the proximal His-170 H^ peaks. The determinationthat one of the most strongly contact-shifted single proton resonances in HRP-I does not arise from the porphyrin dictates that the cation radical must be delocalized to some amino acid residue. The relaxation properties of the non-heme contact-shifted signal in HRP-I support the identity of this contributing residue as the proximal His-170. Detailed analysis of changes in both contact shift pattern and NOEs indicates that compound I formation is accompanied by a~ 5 rotation of the 6-propionate group. The implicationof a porphyrin cation radical delocalized over the proximal histidine for the proposed location of the solely amino acid centered radical in compound I of related cytochrome c peroxidase is discussed.
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辣根过氧化物酶化合物 I 电子结构的质子核磁共振研究。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
LaMar,GN;deRopp,JS;Smith,KM;Langry,KC
通讯作者：
Langry,KC
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影响因子：
15
作者：
V. Thanabal;J. Ropp;G. N. Mar
通讯作者：
G. N. Mar
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DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Lauffer,RB;Antanaitis,BC;Aisen,P;QueJr,L
通讯作者：
QueJr,L
影响因子：
4.8
作者：
T. Yonetani;G. Ray
通讯作者：
G. Ray
DOI：
10.1016/s0021-9258(19)70630-9
发表时间：
1980-09
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
T. Poulos;J. Kraut
通讯作者：
T. Poulos;J. Kraut