Orientation-selected 15N-HYSCORE detection of weakly coupled nitrogens around the archaeal rieske [2Fe-2S] center

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

doi:10.1021/ja045898x

Orientation-selected ¹⁵N-HYSCORE detection of weakly coupled nitrogens around the archaeal rieske [2Fe-2S] center

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

Veterinary Clinical Medicine

Research output: Contribution to journal › Article › peer-review

Abstract

The weakly coupled ¹⁵N atoms around a reduced Rieske [2Fe-2S] cluster of the uniformly ¹⁵N-labeled, hyperthermostable archaeal Rieske protein appear to produce readily observable cross-peaks in the HYSCORE spectra, with the well-resolved couplings of 0.3-0.4 MHz for the N_ε and 1.1 MHz for the peptide backbone nitrogens, in addition to the contributions from the coordinated N_δ atoms. These features can be used for structure-mechanism studies of the biological redox protein system involving the weakly coupled nitrogens in coupled electron-proton transfer reactions.

Original language	English (US)
Pages (from-to)	13902-13903
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	126
Issue number	43
DOIs	https://doi.org/10.1021/ja045898x
State	Published - Nov 3 2004

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja045898x

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title = "Orientation-selected 15N-HYSCORE detection of weakly coupled nitrogens around the archaeal rieske [2Fe-2S] center",

abstract = "The weakly coupled 15N atoms around a reduced Rieske [2Fe-2S] cluster of the uniformly 15N-labeled, hyperthermostable archaeal Rieske protein appear to produce readily observable cross-peaks in the HYSCORE spectra, with the well-resolved couplings of 0.3-0.4 MHz for the Nε and 1.1 MHz for the peptide backbone nitrogens, in addition to the contributions from the coordinated Nδ atoms. These features can be used for structure-mechanism studies of the biological redox protein system involving the weakly coupled nitrogens in coupled electron-proton transfer reactions.",

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AU - Iwasaki, Toshio

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AU - Uzawa, Taketoshi

AU - Samoilova, Rimma I.

AU - Dikanov, Sergei A.

PY - 2004/11/3

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AB - The weakly coupled 15N atoms around a reduced Rieske [2Fe-2S] cluster of the uniformly 15N-labeled, hyperthermostable archaeal Rieske protein appear to produce readily observable cross-peaks in the HYSCORE spectra, with the well-resolved couplings of 0.3-0.4 MHz for the Nε and 1.1 MHz for the peptide backbone nitrogens, in addition to the contributions from the coordinated Nδ atoms. These features can be used for structure-mechanism studies of the biological redox protein system involving the weakly coupled nitrogens in coupled electron-proton transfer reactions.

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