光合放氧复合体催化位点上组氨酸的鉴定。
Identification of histidine at the catalytic site of the photosynthetic oxygen-evolving complex.
作者信息
Tang X S, Diner B A, Larsen B S, Gilchrist M L, Lorigan G A, Britt R D
机构信息
Central Research and Development Department, Experimental Station, E.I. Dupont de Nemours and Company, Wilmington, DE 19880.
出版信息
Proc Natl Acad Sci U S A. 1994 Jan 18;91(2):704-8. doi: 10.1073/pnas.91.2.704.
Abstract
The molecular oxygen in our atmosphere is a product of a water-splitting reaction that occurs in the oxygen-evolving complex of photosystem II of oxygenic photosynthesis. The catalytic core of the oxygen-evolving complex is an ensemble of four manganese atoms arranged in a cluster of undetermined structure. The pulsed electron paramagnetic resonance (EPR) technique of electron spin-echo envelope modulation (ESEEM) can be used to measure nuclear spin transitions of nuclei magnetically coupled to paramagnetic metal centers of enzymes. We report the results of ESEEM experiments on the cyanobacterium Synechocystis PCC 6803 selectively labeled with 15N at the two nitrogen sites of the imidazole side chain of histidine residues. The experiments demonstrate that histidine is bound to manganese in the oxygen-evolving complex.
摘要
我们大气中的分子氧是在含氧光合作用光系统II的放氧复合体中发生的水分解反应的产物。放氧复合体的催化核心是由四个锰原子组成的簇，其结构尚未确定。电子自旋回波包络调制（ESEEM）的脉冲电子顺磁共振（EPR）技术可用于测量与酶的顺磁性金属中心磁耦合的原子核的核自旋跃迁。我们报告了对集胞藻PCC 6803进行ESEEM实验的结果，该集胞藻在组氨酸残基咪唑侧链的两个氮位点选择性地用15N标记。实验表明，组氨酸在放氧复合体中与锰结合。
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