Determination of vinyl orientation in resting state and compound I of horseradish peroxidase by the proton nuclear Overhauser effect
Determination of vinyl orientation in resting state and compound I of horseradish peroxidase by the proton nuclear Overhauser effect
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质子核欧沃豪塞效应测定辣根过氧化物酶静息态乙烯基取向和化合物I
DOI：
10.1021/ja00274a077
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发表时间：
1986
影响因子：
15
通讯作者：
G. N. Mar
中科院分区：
文献类型：
--
作者：
V. Thanabal;J. Ropp;G. N. Mar
大量间接证据表明，辣根过氧化物酶 (HRP) 的血红素袋在立体化学上比肌红蛋白或血红蛋白中的血红素袋更坚硬且更隐蔽。 1 2" 6 这种影响的表现之一是血红素乙烯基的夹紧，从而限制其振荡活动性并迫使其比其他血红素蛋白具有更多的面内取向。 3" 7 这种面内取向已间接得到 NMR3" 5 和共振拉曼、6·7 RR、光谱解释和合理化以增强双氧化反应中间体化合物 I 的稳定性，然而，无法生长足够的单晶，(1)(a) UCD NMR 设施无法进行常规确认。(2) Dunford, B.；Stillman, J. S. Coord. Rev. 1976, 19, 187-251。(3) La Mar, G. N.；Langry, KM；生物化学，1980，255，6646-6652。
There exists a large body of indirect evidence that the heme pocket of horseradish peroxidase, HRP, is stereochemically more rigid and buried than inmyoglobin or hemoglobin. 1 2" 6 One of the manifestations of this influence is the clamping of the heme vinyls so as to restrict their oscillatory mobility and force a more in-plane orientation than in other hemoproteins. 3" 7 Such in-plane orientations have been indirectly supported by both NMR3" 5 and resonance Raman, 6· 7 RR, spectral interpretations and ra-tionalized to enhance the stabilityof the doubly oxidized reactive intermediate, compound I, HRP-I. The inability to grow adequate single crystals, however, has prevented the usual confirmation of (1)(a) Department of Chemistry,(b) UCD NMR Facility.(2) Dunford,. B.; Stillman, J. S. Coord. Chem. Rev. 1976, 19, 187-251.(3) La Mar, G. N.; de Ropp, JS; Smith, KM; Langry, K. CJ Biol. Chem. 1980, 255, 6646-6652.