15N HYSCORE characterization of the fully deprotonated, reduced form of the Archaeal Rieske [2Fe-2S] center

Toshio Iwasaki; Asako Kounosu; Rimma I. Samoilova; Sergei A. Dikanov

doi:10.1021/ja0562393

¹⁵N HYSCORE characterization of the fully deprotonated, reduced form of the Archaeal Rieske [2Fe-2S] center

Toshio Iwasaki, Asako Kounosu, Rimma I. Samoilova, Sergei A. Dikanov

Veterinary Clinical Medicine

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Abstract

The hyperfine couplings for strongly and weakly coupled ¹⁵N nuclei around a reduced Rieske [2Fe-2S] center of uniformly 15N-labeled, hyperthermostable archaeal Rieske protein at pH 13.3 were determined by hyperfine sublevel correlation (HYSCORE) spectroscopy and compared with those at physiological pH. Significant changes in the hyperfine couplings of the terminal histidine N_δ ligands and N_ε nuclei were observed between them, which can be explained by not only the redistribution of the unpaired electron spin density over the ligands but also the difference in the mixed-valence state of the fully deprotonated, reduced cluster. These quantitative data can be used in theoretical analysis for the selection of an appropriate model of the mixed-valence state of the reduced Rieske center at very alkaline pH.

Original language	English (US)
Pages (from-to)	2170-2171
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	7
DOIs	https://doi.org/10.1021/ja0562393
State	Published - Feb 22 2006

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja0562393

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title = "15N HYSCORE characterization of the fully deprotonated, reduced form of the Archaeal Rieske [2Fe-2S] center",

abstract = "The hyperfine couplings for strongly and weakly coupled 15N nuclei around a reduced Rieske [2Fe-2S] center of uniformly 15N-labeled, hyperthermostable archaeal Rieske protein at pH 13.3 were determined by hyperfine sublevel correlation (HYSCORE) spectroscopy and compared with those at physiological pH. Significant changes in the hyperfine couplings of the terminal histidine Nδ ligands and Nε nuclei were observed between them, which can be explained by not only the redistribution of the unpaired electron spin density over the ligands but also the difference in the mixed-valence state of the fully deprotonated, reduced cluster. These quantitative data can be used in theoretical analysis for the selection of an appropriate model of the mixed-valence state of the reduced Rieske center at very alkaline pH.",

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T1 - 15N HYSCORE characterization of the fully deprotonated, reduced form of the Archaeal Rieske [2Fe-2S] center

AU - Iwasaki, Toshio

AU - Kounosu, Asako

AU - Samoilova, Rimma I.

AU - Dikanov, Sergei A.

PY - 2006/2/22

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AB - The hyperfine couplings for strongly and weakly coupled 15N nuclei around a reduced Rieske [2Fe-2S] center of uniformly 15N-labeled, hyperthermostable archaeal Rieske protein at pH 13.3 were determined by hyperfine sublevel correlation (HYSCORE) spectroscopy and compared with those at physiological pH. Significant changes in the hyperfine couplings of the terminal histidine Nδ ligands and Nε nuclei were observed between them, which can be explained by not only the redistribution of the unpaired electron spin density over the ligands but also the difference in the mixed-valence state of the fully deprotonated, reduced cluster. These quantitative data can be used in theoretical analysis for the selection of an appropriate model of the mixed-valence state of the reduced Rieske center at very alkaline pH.

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