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  High-field EPR and ESEEM investigation of the nitrogen quadrupole interaction of nitroxide spin labels in disordered solids: toward differentiation between polarity and proticity matrix effects on protein function

Savitsky, A., Dubinskii, A. A. A., Plato, M., Grishin, Y. A., Zimmermann, H., & Möbius, K. (2008). High-field EPR and ESEEM investigation of the nitrogen quadrupole interaction of nitroxide spin labels in disordered solids: toward differentiation between polarity and proticity matrix effects on protein function. Journal of Physical Chemistry B, 112(30), 9079-9090. doi:10.1021/jp711640p.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-096F-C Versions-Permalink: https://hdl.handle.net/21.11116/0000-0000-DE3F-1
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 Urheber:
Savitsky, Anton, Autor
Dubinskii, Alexander A. A., Autor
Plato, M., Autor
Grishin, Yu. A., Autor
Zimmermann, Herbert1, Autor           
Möbius, Klaus, Autor
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Zusammenfassung: The combination of high-field electron paramagnetic resonance (EPR) with site-directed spin labeling (SDSL) techniques employing nitroxide radicals has turned out to be particularly powerful in revealing subtle changes of the polarity and proticity profiles in proteins enbedded in membranes. This information can be obtained by orientation-selective high-field EPR resolving principal components of the nitroxide Zeeman (g) and hyperfine ( A) tensors of the spin labels attached to specific molecular sites. In contrast to the g- and A-tensors, the (14)N ( I = 1) quadrupole interaction tensor of the nitroxide spin label has not been exploited in EPR for probing effects of the microenvironment of functional protein sites. In this work it is shown that the W-band (95 GHz) high-field electron spin echo envelope modulation (ESEEM) method is well suited for determining with high accuracy the (14)N quadrupole tensor principal components of a nitroxide spin label in disordered frozen solution. By W-band ESEEM the quadrupole components of a five-ring pyrroline-type nitroxide radical in glassy ortho-terphenyl and glycerol solutions have been determined. This radical is the headgroup of the MTS spin label widely used in SDSL protein studies. By DFT calulations and W-band ESEEM experiments it is demonstrated that the Q(yy) value is especially sensitive to the proticity and polarity of the nitroxide environment in H-bonding and nonbonding situations. The quadrupole tensor is shown to be rather insensitive to structural variations of the nitroxide label itself. When using Q(yy) as a testing probe of the environment, its ruggedness toward temperature changes represents an important advantage over the g xx and A(zz) parameters which are usually employed for probing matrix effects on the spin labeled molecular site. Thus, beyond measurenments of g xx and A(zz) of spin labeled protein sites in disordered solids, W-band high-field ESEEM studies of (14)N quadrupole interactions open a new avenue to reliably probe subtle environmental effects on the electronic structure. This is a significant step forward on the way to differentiate between effects from matrix polarity and hydrogen-bond formation.

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Sprache(n): eng - English
 Datum: 2007-12-112008-04-212008-07-022008-07-31
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1021/jp711640p
URI: http://www.ncbi.nlm.nih.gov/pubmed/18593147
 Art des Abschluß: -

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Titel: Journal of Physical Chemistry B
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 112 (30) Artikelnummer: - Start- / Endseite: 9079 - 9090 Identifikator: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370