Standard

ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2. / Isaev, Nikolay; Heuveling, Johanna; Ivanisenko, Nikita et al.

In: Applied Magnetic Resonance, Vol. 50, No. 7, 01.07.2019, p. 883-893.

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

Harvard

Isaev, N, Heuveling, J, Ivanisenko, N, Schneider, E & Steinhoff, HJ 2019, 'ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2', Applied Magnetic Resonance, vol. 50, no. 7, pp. 883-893. https://doi.org/10.1007/s00723-019-01114-y

APA

Isaev, N., Heuveling, J., Ivanisenko, N., Schneider, E., & Steinhoff, H. J. (2019). ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2. Applied Magnetic Resonance, 50(7), 883-893. https://doi.org/10.1007/s00723-019-01114-y

Vancouver

Isaev N, Heuveling J, Ivanisenko N, Schneider E, Steinhoff HJ. ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2. Applied Magnetic Resonance. 2019 Jul 1;50(7):883-893. doi: 10.1007/s00723-019-01114-y

Author

Isaev, Nikolay ; Heuveling, Johanna ; Ivanisenko, Nikita et al. / ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2. In: Applied Magnetic Resonance. 2019 ; Vol. 50, No. 7. pp. 883-893.

BibTeX

@article{2c12bbf5dee54b299a8058858598afd9,
title = "ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2",
abstract = " Localization of substrates in membrane proteins is an important but challenging task. In this paper, we show that deuterium electron spin echo envelope modulation spectroscopy ( 2 H ESEEM) combined with site-directed spin labeling is a powerful tool to localize the substrate, histidine-d5, in the ABC transporter HisQMP 2 . Based on a homology model and spin label rotamer analyses, we calculated 2 H ESEEM spectra for eight possible labeling positions close to the putative substrate-binding site. Experimental 2 H ESEEM spectra were determined with spin labels bound either at position 169 of HisM, for which a detectable 2 H ESEEM signal was calculated, or with a spin label bound at position 54 of HisQ as a negative control. The agreement between the calculated and experimental ESEEM spectra provides strong evidence for the histidine located in a binding site primarily liganded by residues of HisM as proposed by the homology model. ",
keywords = "ELECTRON-SPIN-ECHO, ENVELOPE MODULATION, WATER CONCENTRATION, EPR SPECTROSCOPY, MEMBRANE, BINDING, RADICALS, INVESTIGATE, DIVERSITY, PROTEINS",
author = "Nikolay Isaev and Johanna Heuveling and Nikita Ivanisenko and Erwin Schneider and Steinhoff, {Heinz J{\"u}rgen}",
note = "Publisher Copyright: {\textcopyright} 2019, Springer-Verlag GmbH Austria, part of Springer Nature.",
year = "2019",
month = jul,
day = "1",
doi = "10.1007/s00723-019-01114-y",
language = "English",
volume = "50",
pages = "883--893",
journal = "Applied Magnetic Resonance",
issn = "0937-9347",
publisher = "Springer-Verlag GmbH and Co. KG",
number = "7",

}

RIS

TY - JOUR

T1 - ESEEM Reveals Bound Substrate Histidine in the ABC Transporter HisQMP 2

AU - Isaev, Nikolay

AU - Heuveling, Johanna

AU - Ivanisenko, Nikita

AU - Schneider, Erwin

AU - Steinhoff, Heinz Jürgen

N1 - Publisher Copyright: © 2019, Springer-Verlag GmbH Austria, part of Springer Nature.

PY - 2019/7/1

Y1 - 2019/7/1

N2 - Localization of substrates in membrane proteins is an important but challenging task. In this paper, we show that deuterium electron spin echo envelope modulation spectroscopy ( 2 H ESEEM) combined with site-directed spin labeling is a powerful tool to localize the substrate, histidine-d5, in the ABC transporter HisQMP 2 . Based on a homology model and spin label rotamer analyses, we calculated 2 H ESEEM spectra for eight possible labeling positions close to the putative substrate-binding site. Experimental 2 H ESEEM spectra were determined with spin labels bound either at position 169 of HisM, for which a detectable 2 H ESEEM signal was calculated, or with a spin label bound at position 54 of HisQ as a negative control. The agreement between the calculated and experimental ESEEM spectra provides strong evidence for the histidine located in a binding site primarily liganded by residues of HisM as proposed by the homology model.

AB - Localization of substrates in membrane proteins is an important but challenging task. In this paper, we show that deuterium electron spin echo envelope modulation spectroscopy ( 2 H ESEEM) combined with site-directed spin labeling is a powerful tool to localize the substrate, histidine-d5, in the ABC transporter HisQMP 2 . Based on a homology model and spin label rotamer analyses, we calculated 2 H ESEEM spectra for eight possible labeling positions close to the putative substrate-binding site. Experimental 2 H ESEEM spectra were determined with spin labels bound either at position 169 of HisM, for which a detectable 2 H ESEEM signal was calculated, or with a spin label bound at position 54 of HisQ as a negative control. The agreement between the calculated and experimental ESEEM spectra provides strong evidence for the histidine located in a binding site primarily liganded by residues of HisM as proposed by the homology model.

KW - ELECTRON-SPIN-ECHO

KW - ENVELOPE MODULATION

KW - WATER CONCENTRATION

KW - EPR SPECTROSCOPY

KW - MEMBRANE

KW - BINDING

KW - RADICALS

KW - INVESTIGATE

KW - DIVERSITY

KW - PROTEINS

UR - http://www.scopus.com/inward/record.url?scp=85061999959&partnerID=8YFLogxK

U2 - 10.1007/s00723-019-01114-y

DO - 10.1007/s00723-019-01114-y

M3 - Article

AN - SCOPUS:85061999959

VL - 50

SP - 883

EP - 893

JO - Applied Magnetic Resonance

JF - Applied Magnetic Resonance

SN - 0937-9347

IS - 7

ER -

ID: 18623393