EPR spectroscopy of iron−sulfur proteins
作者： Wilfred R. Hagen
DOI: 10.1016/S0898-8838(08)60064-1
关键词: Coordination sphere 、 Metal 、 Chemistry 、 Nuclear magnetic resonance 、 Principal axis theorem 、 Metalloprotein 、 Crystallography 、 Electron paramagnetic resonance 、 Levorotatory 、 Heme 、 Spectroscopy
摘要: Publisher Summary This chapter describes electron paramagnetic resonance (EPR) spectroscopy of iron–sulfur proteins. The first EPR experiments on biological systems were carried out along the same lines. Many spectra taken as a function orientation magnetic field with respect to axes hemoglobin crystals frozen in their mother liquor. g-tensor principal crystal axis was determined. Later, X-ray structures available, found approximately correspond heme plane and normal. Detailed information haem may be combined measurements calculate polypeptide chain directions similar factors. A metal site formally does not have any symmetry at all, if only because it is ligated by made up levorotatory amino acid residues. especially true when protein ligation forms part coordination sphere,
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