用单晶 EPR 光谱法分析固氮酶 FeMo 辅因子的磁性。
Analysis of the magnetic properties of nitrogenase FeMo cofactor by single-crystal EPR spectroscopy.
机构信息
Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://portal.uni-freiburg.de/biochemie; BIOSS Centre for Biological Signalling Studies, Hebelstrasse 25, 79104 Freiburg (Germany); Present address: Howard Hughes Medical Institute (HHMI) and Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena CA 91125 (USA).
出版信息
Angew Chem Int Ed Engl. 2013 Sep 16;52(38):10116-9. doi: 10.1002/anie.201303000. Epub 2013 Aug 8.
The catalytic center of nitrogenase, the [Mo:7Fe:9S:C]:homocitrate FeMo cofactor, is a S=3/2 system with a rhombic magnetic g tensor. Single-crystal EPR spectroscopy in combination with X-ray diffraction were used to determine the relative orientation of the g tensor with respect to the cluster structure. The protein environment influences the electronic structure of the FeMo cofactor, dictating preferred orientations of possible functional relevance.
固氮酶的催化中心，即 [Mo:7Fe:9S:C]:同型柠檬酸铁钼辅因子，是一个 S=3/2 系统，具有菱形磁 g 张量。单晶电子顺磁共振波谱学与 X 射线衍射相结合，用于确定 g 张量相对于簇结构的相对取向。蛋白质环境会影响 FeMo 辅因子的电子结构，决定可能具有功能相关性的优先取向。
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