EPR spectroscopy as a probe of metal centres in biological systems.
Molecular paramagnetism pervades the bioinorganic chemistry of V, Mn, Fe, Co, Ni, Cu, Mo, W, and of a number of non-biological transition elements. To date we can look back at half a century of fruitful EPR studies on metalloproteins, and against this background evaluate the significance of modern EPR spectroscopy from the perspective of a biochemist, making a distinction between conventional continuous wave X-band spectroscopy as a reliable work horse with broad, established applicability even on crude preparations, vs. a diffuse set of "advanced EPR" technologies whose practical application typically calls for narrowly focused research hypotheses and very high quality samples. The type of knowledge on metalloproteins that is readily obtainable with EPR spectroscopy, is explained with illustrative examples, as is the relation between experimental complexity and the spin value of the system.
Hagen
Wilfred R
WR
Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628, BC Delft, The Netherlands. w.r.hagen@tudelft.nl
D004578:Electron Spin Resonance Spectroscopy; D008667:Metalloproteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry*; D015336:Molecular Probe Techniques; D028561:Transition Elements
D008667:Metalloproteins; D008670:Metals; D028561:Transition Elements