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Type: Journal article
Title: Structural information from orientationally selective DEER spectroscopy
Author: Lovett, J.
Bowen, A.
Timmel, C.
Jones, M.
Dilworth, J.
Caprotti, D.
Bell, S.
Wong, L.
Harmer, J.
Citation: Physical Chemistry Chemical Physics, 2009; 11(31):6840-6848
Publisher: Royal Soc Chemistry
Issue Date: 2009
ISSN: 1463-9076
Statement of
J. E. Lovett, A. M. Bowen, C. R. Timmel, M. W. Jones, J. R. Dilworth, D. Caprotti, S. G. Bell, L. L. Wong and J. Harmer
Abstract: Double electron–electron resonance (DEER) spectroscopy can determine, from measurement of the dipolar interaction, the distance and orientation between two paramagnetic centres in systems lacking long-range order such as powders or frozen solution samples. In spin systems with considerable anisotropy, the microwave pulses excite only a fraction of the electron paramagnetic resonance (EPR) spectrum and the resulting orientation selection needs to be explicitly taken into account if a meaningful distance and orientation is to be determined. Here, a general method is presented to analyze the dipolar interaction between two paramagnetic spin centres from a series of DEER traces recorded so that different orientations of the spin–spin vector are sampled. Delocalised spin density distributions and spin projection factors (as for example in iron–sulfur clusters), are explicitly included. Application of the analysis to a spin-labelled flavoprotein reductase/reduced iron–sulfur ferredoxin protein complex and a bi-radical with two Cu(II) ions provides distance and orientation information between the radical centres. In the protein complex this enables the protein–protein binding geometry to be defined. Experimentally, orientationally selective DEER measurements are possible on paramagnetic systems where the resonator bandwidth allows the frequencies of pump and detection pulses to be separated sufficiently to excite enough orientations to define adequately the spin–spin vector.
Keywords: Rhodopseudomonas; Copper; Metalloporphyrins; Hydrogenase; Ferredoxins; Electron Spin Resonance Spectroscopy; Molecular Conformation; Protein Conformation; Protein Binding; Algorithms; Models, Molecular
Rights: Copyright the Authors
RMID: 0020121281
DOI: 10.1039/B907010A
Appears in Collections:Chemistry publications

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