Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes.
Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes.
复制标题
通过一氧化碳复合物的碳 13 核磁共振波谱比较过氧化物酶和其他血红素蛋白中的血红素环境和近端配体。
DOI：
10.1016/0006-291x(85)91280-x
复制
发表时间：
1985
影响因子：
3.1
通讯作者：
Goff,HM
中科院分区：
文献类型：
--
作者：
Behere,DV;Gonzalez-Vergara,E;Goff,HM
Carbon-13 nuclear magnetic resonance signals for the carbon monoxide ligand in ferrous complexes of horseradish peroxidase, lactoperoxidase, and chloroperoxidase are located respectively at 209.1, 208.3, and 200.8 parts per million from the tetramethylsilane reference. On the basis of previous hemoprotein and model compound studies these resonance positions are consistent with coordination of a proximal histidine ligand in horseradish peroxidase and lactoperoxidase, and coordination of a cysteinyl mercaptide ligand in chloroperoxidase. Carbonyl chemical shift values for acidic and basic horseradish peroxidase isoenzymes are very similar.
