Comparison of the heme electronic and molecular structure of soybean leghemoglobin and sperm whale myoglobin by proton NMR.
Comparison of the heme electronic and molecular structure of soybean leghemoglobin and sperm whale myoglobin by proton NMR.
复制标题
通过质子核磁共振比较大豆豆血红蛋白和抹香鲸肌红蛋白的血红素电子和分子结构。
DOI：
10.1016/0006-291x(81)91500-x
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发表时间：
1981
影响因子：
3.1
通讯作者：
Langry,KC
中科院分区：
文献类型：
--
作者：
LaMar,GN;Kong,SB;Smith,KM;Langry,KC
用血红素甲基的特异性氘代反应对低自旋氰化物和烟酸盐络合物中大豆铁豆血红蛋白a的质子核磁共振谱进行了归属。的分配不同，从核Overhauser增强测量仅获得的，并指示近端组氨酰咪唑-氯化血红素的相互作用，这是非常相似的抹香鲸肌红蛋白中发现的。豆血红蛋白中远端组氨酸的超精细移位可交换NH峰的存在表明该远端配体的取向非常不同，或者与肌红蛋白中发现的散装溶剂的交换速率显著更快。
The proton nuclear magnetic resonance spectra of soybean ferric leghemoglobin a in the low-spin cyanide and nicotinate complexes have been assigned by specific deuteration of heme methyl groups. The assignments differ from those obtained solely from nuclear Overhauser enhancement measurements and are indicative of a proximal histidyl imidazole-hemin interaction which is very similar to that found in sperm whale myoglobin. The absence of a hyperfine shifted exchangeable NH peak for the distal histidine in leghemoglobin suggests either a very different orientation for this distal ligand or a significantly faster exchange rate with bulk solvent than found in myoglobin.