Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from AgI to CdII
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Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from AgI to CdII. / Balogh, Ria K.; Gyurcsik, Béla; Jensen, Mikael; Thulstrup, Peter W.; Köster, Ulli; Christensen, Niels Johan; Mørch, Frederik J.; Jensen, Marianne L.; Jancsó, Attila; Hemmingsen, Lars.
In: Chemistry: A European Journal, Vol. 26, No. 33, 2020, p. 7451-7457.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from AgI to CdII
AU - Balogh, Ria K.
AU - Gyurcsik, Béla
AU - Jensen, Mikael
AU - Thulstrup, Peter W.
AU - Köster, Ulli
AU - Christensen, Niels Johan
AU - Mørch, Frederik J.
AU - Jensen, Marianne L.
AU - Jancsó, Attila
AU - Hemmingsen, Lars
PY - 2020
Y1 - 2020
N2 - Selectivity for monovalent metal ions is an important facet of the function of the metalloregulatory protein CueR. 111Ag perturbed angular correlation of γ‐rays (PAC) spectroscopy probes the metal site structure and the relaxation accompanying the instantaneous change from AgI to CdII upon 111Ag radioactive decay. That is, a change from AgI, which activates transcription, to CdII, which does not. In the frozen state (−196 °C) two nuclear quadrupole interactions (NQIs) are observed; one (NQI1) agrees well with two coordinating thiolates and an additional longer contact to the S77 backbone carbonyl, and the other (NQI2) reflects that CdII has attracted additional ligand(s). At 1 °C only NQI2 is observed, demonstrating that relaxation to this structure occurs within ≈10 ns of the decay of 111Ag. Thus, transformation from AgI to CdII rapidly disrupts the functional linear bis(thiolato)AgI metal site structure. This inherent metal site flexibility may be central to CueR function, leading to remodelling into a non‐functional structure upon binding of non‐cognate metal ions. In a broader perspective, 111Ag PAC spectroscopy may be applied to probe the flexibility of protein metal sites.
AB - Selectivity for monovalent metal ions is an important facet of the function of the metalloregulatory protein CueR. 111Ag perturbed angular correlation of γ‐rays (PAC) spectroscopy probes the metal site structure and the relaxation accompanying the instantaneous change from AgI to CdII upon 111Ag radioactive decay. That is, a change from AgI, which activates transcription, to CdII, which does not. In the frozen state (−196 °C) two nuclear quadrupole interactions (NQIs) are observed; one (NQI1) agrees well with two coordinating thiolates and an additional longer contact to the S77 backbone carbonyl, and the other (NQI2) reflects that CdII has attracted additional ligand(s). At 1 °C only NQI2 is observed, demonstrating that relaxation to this structure occurs within ≈10 ns of the decay of 111Ag. Thus, transformation from AgI to CdII rapidly disrupts the functional linear bis(thiolato)AgI metal site structure. This inherent metal site flexibility may be central to CueR function, leading to remodelling into a non‐functional structure upon binding of non‐cognate metal ions. In a broader perspective, 111Ag PAC spectroscopy may be applied to probe the flexibility of protein metal sites.
U2 - 10.1002/chem.202000132
DO - 10.1002/chem.202000132
M3 - Journal article
C2 - 32045037
VL - 26
SP - 7451
EP - 7457
JO - Chemistry: A European Journal
JF - Chemistry: A European Journal
SN - 0947-6539
IS - 33
ER -
ID: 241995340