Standard

EPR evidence for a fast-relaxing iron center in Na+-translocating NADH : quinone-oxidoreductase. / Kulik, Leonid V.; Bertsova, Yulia V.; Bogachev, Alexander V.

в: Journal of Inorganic Biochemistry, Том 184, 01.07.2018, стр. 15-18.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Kulik, LV, Bertsova, YV & Bogachev, AV 2018, 'EPR evidence for a fast-relaxing iron center in Na+-translocating NADH: quinone-oxidoreductase', Journal of Inorganic Biochemistry, Том. 184, стр. 15-18. https://doi.org/10.1016/j.jinorgbio.2018.04.004

APA

Kulik, L. V., Bertsova, Y. V., & Bogachev, A. V. (2018). EPR evidence for a fast-relaxing iron center in Na+-translocating NADH: quinone-oxidoreductase. Journal of Inorganic Biochemistry, 184, 15-18. https://doi.org/10.1016/j.jinorgbio.2018.04.004

Vancouver

Kulik LV, Bertsova YV, Bogachev AV. EPR evidence for a fast-relaxing iron center in Na+-translocating NADH: quinone-oxidoreductase. Journal of Inorganic Biochemistry. 2018 июль 1;184:15-18. doi: 10.1016/j.jinorgbio.2018.04.004

Author

Kulik, Leonid V. ; Bertsova, Yulia V. ; Bogachev, Alexander V. / EPR evidence for a fast-relaxing iron center in Na+-translocating NADH : quinone-oxidoreductase. в: Journal of Inorganic Biochemistry. 2018 ; Том 184. стр. 15-18.

BibTeX

@article{8eef50c6a7e34e81a045f6555fd1fd11,
title = "EPR evidence for a fast-relaxing iron center in Na+-translocating NADH: quinone-oxidoreductase",
abstract = "A paramagnetic Cys4[Fe] center was detected by pulse EPR in Na+-translocating NADH:quinone-oxidoreductase (Na+-NQR) by influence of this center on transverse and longitudinal spin relaxation of Na+-NQR flavin radicals. The oxidation state of the Cys4[Fe] center was Fe3+ in the oxidized and Fe2+ in the reduced Na+-NQR, as deduced from the temperature dependence of spin relaxation rates of different flavin radicals. A high-spin state of iron in the Cys4[Fe] center was assigned to both forms of Na+-NQR.",
keywords = "Electron paramagnetic resonance, Flavin radicals, Mononuclear iron center, NADH:quinone oxidoreductase, Spin relaxation, Electron Spin Resonance Spectroscopy/methods, Temperature, Oxidation-Reduction, Bacterial Proteins/chemistry, NAD(P)H Dehydrogenase (Quinone)/chemistry, Iron/chemistry",
author = "Kulik, {Leonid V.} and Bertsova, {Yulia V.} and Bogachev, {Alexander V.}",
note = "Publisher Copyright: {\textcopyright} 2018 Elsevier Inc.",
year = "2018",
month = jul,
day = "1",
doi = "10.1016/j.jinorgbio.2018.04.004",
language = "English",
volume = "184",
pages = "15--18",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Science Inc.",

}

RIS

TY - JOUR

T1 - EPR evidence for a fast-relaxing iron center in Na+-translocating NADH

T2 - quinone-oxidoreductase

AU - Kulik, Leonid V.

AU - Bertsova, Yulia V.

AU - Bogachev, Alexander V.

N1 - Publisher Copyright: © 2018 Elsevier Inc.

PY - 2018/7/1

Y1 - 2018/7/1

N2 - A paramagnetic Cys4[Fe] center was detected by pulse EPR in Na+-translocating NADH:quinone-oxidoreductase (Na+-NQR) by influence of this center on transverse and longitudinal spin relaxation of Na+-NQR flavin radicals. The oxidation state of the Cys4[Fe] center was Fe3+ in the oxidized and Fe2+ in the reduced Na+-NQR, as deduced from the temperature dependence of spin relaxation rates of different flavin radicals. A high-spin state of iron in the Cys4[Fe] center was assigned to both forms of Na+-NQR.

AB - A paramagnetic Cys4[Fe] center was detected by pulse EPR in Na+-translocating NADH:quinone-oxidoreductase (Na+-NQR) by influence of this center on transverse and longitudinal spin relaxation of Na+-NQR flavin radicals. The oxidation state of the Cys4[Fe] center was Fe3+ in the oxidized and Fe2+ in the reduced Na+-NQR, as deduced from the temperature dependence of spin relaxation rates of different flavin radicals. A high-spin state of iron in the Cys4[Fe] center was assigned to both forms of Na+-NQR.

KW - Electron paramagnetic resonance

KW - Flavin radicals

KW - Mononuclear iron center

KW - NADH:quinone oxidoreductase

KW - Spin relaxation

KW - Electron Spin Resonance Spectroscopy/methods

KW - Temperature

KW - Oxidation-Reduction

KW - Bacterial Proteins/chemistry

KW - NAD(P)H Dehydrogenase (Quinone)/chemistry

KW - Iron/chemistry

UR - http://www.scopus.com/inward/record.url?scp=85056461409&partnerID=8YFLogxK

U2 - 10.1016/j.jinorgbio.2018.04.004

DO - 10.1016/j.jinorgbio.2018.04.004

M3 - Article

C2 - 29635097

AN - SCOPUS:85056461409

VL - 184

SP - 15

EP - 18

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

ER -

ID: 17471511