Specificity of the metalloregulator CueR for monovalent metal ions: possible functional role of a coordinated thiol?

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Specificity of the metalloregulator CueR for monovalent metal ions : possible functional role of a coordinated thiol? / Szunyogh, Dániel; Szokolai, Hajnalka; Thulstrup, Peter Waaben; Larsen, Flemming Hofmann; Gyurcsik, Béla; Christensen, Niels Johan; Stachura, Monika Kinga; Hemmingsen, Lars Bo Stegeager; Jancsó, Attila.

I: Angewandte Chemie International Edition, Bind 54, Nr. 52, 2015, s. 15756-15761.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Szunyogh, D, Szokolai, H, Thulstrup, PW, Larsen, FH, Gyurcsik, B, Christensen, NJ, Stachura, MK, Hemmingsen, LBS & Jancsó, A 2015, 'Specificity of the metalloregulator CueR for monovalent metal ions: possible functional role of a coordinated thiol?', Angewandte Chemie International Edition, bind 54, nr. 52, s. 15756-15761. https://doi.org/10.1002/anie.201508555

APA

Szunyogh, D., Szokolai, H., Thulstrup, P. W., Larsen, F. H., Gyurcsik, B., Christensen, N. J., Stachura, M. K., Hemmingsen, L. B. S., & Jancsó, A. (2015). Specificity of the metalloregulator CueR for monovalent metal ions: possible functional role of a coordinated thiol? Angewandte Chemie International Edition, 54(52), 15756-15761. https://doi.org/10.1002/anie.201508555

Vancouver

Szunyogh D, Szokolai H, Thulstrup PW, Larsen FH, Gyurcsik B, Christensen NJ o.a. Specificity of the metalloregulator CueR for monovalent metal ions: possible functional role of a coordinated thiol? Angewandte Chemie International Edition. 2015;54(52):15756-15761. https://doi.org/10.1002/anie.201508555

Author

Szunyogh, Dániel ; Szokolai, Hajnalka ; Thulstrup, Peter Waaben ; Larsen, Flemming Hofmann ; Gyurcsik, Béla ; Christensen, Niels Johan ; Stachura, Monika Kinga ; Hemmingsen, Lars Bo Stegeager ; Jancsó, Attila. / Specificity of the metalloregulator CueR for monovalent metal ions : possible functional role of a coordinated thiol?. I: Angewandte Chemie International Edition. 2015 ; Bind 54, Nr. 52. s. 15756-15761.

Bibtex

@article{06ba437824fb49fb80f9d5f7118cec50,
title = "Specificity of the metalloregulator CueR for monovalent metal ions: possible functional role of a coordinated thiol?",
abstract = "Metal-ion-responsive transcriptional regulators within the MerR family effectively discriminate between mono- and divalent metal ions. Herein we address the origin of the specificity of the CueR protein for monovalent metal ions. Several spectroscopic techniques were employed to study Ag(I) , Zn(II) , and Hg(II) binding to model systems encompassing the metal-ion-binding loop of CueR from E. coli and V. cholerae. In the presence of Ag(I) , a conserved cysteine residue displays a pKa value for deprotonation of the thiol that is close to the physiological pH value. This property is only observed with the monovalent metal ion. Quantum chemically optimized structures of the CueR metal site with Cys 112 protonated demonstrate that the conserved Ser 77 backbone carbonyl oxygen atom from the other monomer of the homodimer is {"}pulled{"} towards the metal site. A common allosteric mechanism of the metalloregulatory members of the MerR family is proposed. For CueR, the mechanism relies on the protonation of Cys 112.",
author = "D{\'a}niel Szunyogh and Hajnalka Szokolai and Thulstrup, {Peter Waaben} and Larsen, {Flemming Hofmann} and B{\'e}la Gyurcsik and Christensen, {Niels Johan} and Stachura, {Monika Kinga} and Hemmingsen, {Lars Bo Stegeager} and Attila Jancs{\'o}",
note = "{\textcopyright} 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2015",
doi = "10.1002/anie.201508555",
language = "English",
volume = "54",
pages = "15756--15761",
journal = "Angewandte Chemie International Edition",
issn = "1433-7851",
publisher = "Wiley-VCH Verlag GmbH & Co. KGaA",
number = "52",

}

RIS

TY - JOUR

T1 - Specificity of the metalloregulator CueR for monovalent metal ions

T2 - possible functional role of a coordinated thiol?

AU - Szunyogh, Dániel

AU - Szokolai, Hajnalka

AU - Thulstrup, Peter Waaben

AU - Larsen, Flemming Hofmann

AU - Gyurcsik, Béla

AU - Christensen, Niels Johan

AU - Stachura, Monika Kinga

AU - Hemmingsen, Lars Bo Stegeager

AU - Jancsó, Attila

N1 - © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PY - 2015

Y1 - 2015

N2 - Metal-ion-responsive transcriptional regulators within the MerR family effectively discriminate between mono- and divalent metal ions. Herein we address the origin of the specificity of the CueR protein for monovalent metal ions. Several spectroscopic techniques were employed to study Ag(I) , Zn(II) , and Hg(II) binding to model systems encompassing the metal-ion-binding loop of CueR from E. coli and V. cholerae. In the presence of Ag(I) , a conserved cysteine residue displays a pKa value for deprotonation of the thiol that is close to the physiological pH value. This property is only observed with the monovalent metal ion. Quantum chemically optimized structures of the CueR metal site with Cys 112 protonated demonstrate that the conserved Ser 77 backbone carbonyl oxygen atom from the other monomer of the homodimer is "pulled" towards the metal site. A common allosteric mechanism of the metalloregulatory members of the MerR family is proposed. For CueR, the mechanism relies on the protonation of Cys 112.

AB - Metal-ion-responsive transcriptional regulators within the MerR family effectively discriminate between mono- and divalent metal ions. Herein we address the origin of the specificity of the CueR protein for monovalent metal ions. Several spectroscopic techniques were employed to study Ag(I) , Zn(II) , and Hg(II) binding to model systems encompassing the metal-ion-binding loop of CueR from E. coli and V. cholerae. In the presence of Ag(I) , a conserved cysteine residue displays a pKa value for deprotonation of the thiol that is close to the physiological pH value. This property is only observed with the monovalent metal ion. Quantum chemically optimized structures of the CueR metal site with Cys 112 protonated demonstrate that the conserved Ser 77 backbone carbonyl oxygen atom from the other monomer of the homodimer is "pulled" towards the metal site. A common allosteric mechanism of the metalloregulatory members of the MerR family is proposed. For CueR, the mechanism relies on the protonation of Cys 112.

U2 - 10.1002/anie.201508555

DO - 10.1002/anie.201508555

M3 - Journal article

C2 - 26563985

VL - 54

SP - 15756

EP - 15761

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

SN - 1433-7851

IS - 52

ER -

ID: 147925064