Abstract
An electron spin echo-detected electron paramagnetic resonance study has been performed on the type-2 copper site of the nitrite reductase from Alcaligenes faecalis. The experiment on a single crystal at 95 GHz has allowed the determination of the complete g tensor. This includes the orientations of the principal axes of three g tensors in the asymmetric unit of the unit cell with respect to the crystallographic axes. The orientation with respect to the crystallographic axes has been translated into the orientation of the g tensor in the type-2 copper site. The corresponding electronic structure is discussed in relation to the enzymatic function of this copper site.
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Acknowledgments
This work was supported with financial aid by The Netherlands Organization for Scientific Research (NWO), Department of Chemical Sciences (CW), and by a Natural Sciences and Engineering Research Council of Canada Discovery Grant and the Canadian Foundation for Innovation (to M. E. P. M.).
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This paper is dedicated to Giovanni Giacometti on the occasion of his 85th birthday.
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Scarpelli, F., Arrieta, A.L., Gast, P. et al. A Single-Crystal EPR Study at 95 GHz of the Type-2 Copper Site of Nitrite Reductase From Alcaligenes faecalis . Appl Magn Reson 46, 411–420 (2015). https://doi.org/10.1007/s00723-014-0628-1
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DOI: https://doi.org/10.1007/s00723-014-0628-1