A Single-Crystal EPR Study at 95 GHz of the Type-2 Copper Site of Nitrite Reductase From Alcaligenes faecalis

• Published in: Applied magnetic resonance Vol. 46; no. 4; pp. 411 - 420
• Main Authors: Scarpelli, F., Arrieta, A. L., Gast, P., Groenen, E. J. J., Milikisyants, S., Murphy, M. E. P., Huber, M.
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 01.04.2015; Springer Nature B.V
• Subjects: Atoms and Molecules in Strong Fields; Copper; Crystallography; Electron paramagnetic resonance; Electron spin; Electronic structure; Electrons; Enzymes; Laser Matter Interaction; Ligands; Magnetic fields; Mathematical analysis; Organic Chemistry; Physical Chemistry; Physics; Physics and Astronomy; Proteins; Reductases; Single crystals; Solid State Physics; Spectroscopy/Spectrometry; Spectrum analysis; Tensors; Unit cell; High Occupied Molecular Orbital; Nitrite Reductase; Electron Paramagnetic Resonance Study; Electron Paramagnetic Resonance; Electron Paramagnetic Resonance Spectrum
• ISSN: 0937-9347; 1613-7507
• DOI: 10.1007/s00723-014-0628-1

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.