去1-41轻链激活的牛血浆蛋白C的二价阳离子结合位点与连接到活性位点丝氨酸残基上的氮氧化物自旋标记之间距离的估计。
Estimation of the distance between the divalent cation binding site of des-1-41-light chain-activated bovine plasma protein C and a nitroxide spin label attached to the active-site serine residue.
作者信息
Hill K A, Steiner S A, Castellino F J
机构信息
Department of Chemistry, University of Notre Dame, IN 46556.
出版信息
Biochem J. 1988 Apr 1;251(1):229-36. doi: 10.1042/bj2510229.
The paramagnetic effect of Mn2+ on the electron paramagnetic resonance spectrum of a nitroxide spin label covalently attached to the active-site serine residue of des-1-41-light chain bovine plasma-activated protein C, and situated at a distance of approximately 1.2 nm from this amino acid, has been utilized to estimate the distance on the enzyme surface between the single Mn2+ site and the free electron of the spin label. This distance has been found to be approx. 1.12 nm. A significant paramagnetic effect of Mn2+ on the spectrum of this same nitroxide spin label bound to activated protein C (APC) has been found. However, in this case distance calculations are complicated by the existence of a multiplicity of Mn2+ sites on APC. If it is assumed that a single Mn2+ site is responsible for the paramagnetic effect on the spectrum of the spin label, the interelectron distance on APC would be approx. 0.90 nm.
利用Mn²⁺对共价连接到去1-41轻链牛血浆活化蛋白C活性位点丝氨酸残基上、且与该氨基酸相距约1.2 nm的氮氧自旋标记电子顺磁共振谱的顺磁效应，来估算酶表面单个Mn²⁺位点与自旋标记自由电子之间的距离。已发现该距离约为1.12 nm。还发现Mn²⁺对结合到活化蛋白C（APC）上的同一氮氧自旋标记的谱有显著顺磁效应。然而，在这种情况下，由于APC上存在多个Mn²⁺位点，距离计算变得复杂。如果假设单个Mn²⁺位点对自旋标记谱的顺磁效应负责，那么APC上的电子间距离约为0.90 nm。
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