EPR evidence for a fast-relaxing iron center in Na+-translocating NADH: quinone-oxidoreductase

Leonid V. Kulik; Yulia V. Bertsova; Alexander V. Bogachev

doi:10.1016/j.jinorgbio.2018.04.004

EPR evidence for a fast-relaxing iron center in Na⁺-translocating NADH: quinone-oxidoreductase

Leonid V. Kulik, Yulia V. Bertsova, Alexander V. Bogachev

Laboratory for Structures and Functional Properties of Molecular Systems

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

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.

Original language	English
Pages (from-to)	15-18
Number of pages	4
Journal	Journal of Inorganic Biochemistry
Volume	184
DOIs	https://doi.org/10.1016/j.jinorgbio.2018.04.004
Publication status	Published - 1 Jul 2018

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

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10.1016/j.jinorgbio.2018.04.004

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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.}",

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.",

}

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.

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 -

EPR evidence for a fast-relaxing iron center in Na⁺-translocating NADH: quinone-oxidoreductase

Abstract

Keywords

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