Artificial Metalloproteins for Binding and Stabilization of a Semiquinone Radical

Nathalie Ségaud; Ivana Drienovská; Juan Chen; Wesley R. Browne; Gerard Roelfes

doi:10.1021/acs.inorgchem.7b02073

Artificial Metalloproteins for Binding and Stabilization of a Semiquinone Radical

Nathalie Ségaud, Ivana Drienovská, Juan Chen, Wesley R. Browne, Gerard Roelfes^*

^*Corresponding author for this work

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

The interaction of a number of first-row transition-metal ions with a 2,2′-bipyridyl alanine (bpyA) unit incorporated into the lactococcal multidrug resistance regulator (LmrR) scaffold is reported. The composition of the active site is shown to influence binding affinities. In the case of Fe(II), we demonstrate the need of additional ligating residues, in particular those containing carboxylate groups, in the vicinity of the binding site. Moreover, stabilization of di-tert-butylsemiquinone radical (DTB-SQ) in water was achieved by binding to the designed metalloproteins, which resulted in the radical being shielded from the aqueous environment. This allowed the first characterization of the radical semiquinone in water by resonance Raman spectroscopy.

Original language	English
Pages (from-to)	13293-13299
Number of pages	7
Journal	Inorganic Chemistry
Volume	56
Issue number	21
DOIs	https://doi.org/10.1021/acs.inorgchem.7b02073
Publication status	Published - 6 Nov 2017
Externally published	Yes

Funding

This project was supported by the European Research Council (ERC starting grant no. 280010) and The Netherlands Organisation for Scientific Research (Vici grant, 724.013.003). G.R. and W.R.B. acknowledge support from the Ministry of Education, Culture and Science (Gravity programme no. 024.001.035). J.C. acknowledges the China Scholarship Council (CSC). The authors thank Prof. P. G. Schultz (The Scripps Research Institute) for kindly providing the pEVOL plasmid for in vivo incorporation of bpyA.

Funders	Funder number
Seventh Framework Programme	280010
European Research Council
Ministerie van Onderwijs, Cultuur en Wetenschap	024.001.035
Nederlandse Organisatie voor Wetenschappelijk Onderzoek	724.013.003
China Scholarship Council

Access to Document

10.1021/acs.inorgchem.7b02073

Persistent URL (handle)

Copy link address

Cite this

@article{b01c125d6b064cc3a4c357ed5ed38344,

title = "Artificial Metalloproteins for Binding and Stabilization of a Semiquinone Radical",

abstract = "The interaction of a number of first-row transition-metal ions with a 2,2′-bipyridyl alanine (bpyA) unit incorporated into the lactococcal multidrug resistance regulator (LmrR) scaffold is reported. The composition of the active site is shown to influence binding affinities. In the case of Fe(II), we demonstrate the need of additional ligating residues, in particular those containing carboxylate groups, in the vicinity of the binding site. Moreover, stabilization of di-tert-butylsemiquinone radical (DTB-SQ) in water was achieved by binding to the designed metalloproteins, which resulted in the radical being shielded from the aqueous environment. This allowed the first characterization of the radical semiquinone in water by resonance Raman spectroscopy.",

author = "Nathalie S{\'e}gaud and Ivana Drienovsk{\'a} and Juan Chen and Browne, {Wesley R.} and Gerard Roelfes",

year = "2017",

month = nov,

day = "6",

doi = "10.1021/acs.inorgchem.7b02073",

language = "English",

volume = "56",

pages = "13293--13299",

journal = "Inorganic Chemistry",

issn = "0020-1669",

publisher = "American Chemical Society",

number = "21",

}

TY - JOUR

T1 - Artificial Metalloproteins for Binding and Stabilization of a Semiquinone Radical

AU - Ségaud, Nathalie

AU - Drienovská, Ivana

AU - Chen, Juan

AU - Browne, Wesley R.

AU - Roelfes, Gerard

PY - 2017/11/6

Y1 - 2017/11/6

N2 - The interaction of a number of first-row transition-metal ions with a 2,2′-bipyridyl alanine (bpyA) unit incorporated into the lactococcal multidrug resistance regulator (LmrR) scaffold is reported. The composition of the active site is shown to influence binding affinities. In the case of Fe(II), we demonstrate the need of additional ligating residues, in particular those containing carboxylate groups, in the vicinity of the binding site. Moreover, stabilization of di-tert-butylsemiquinone radical (DTB-SQ) in water was achieved by binding to the designed metalloproteins, which resulted in the radical being shielded from the aqueous environment. This allowed the first characterization of the radical semiquinone in water by resonance Raman spectroscopy.

AB - The interaction of a number of first-row transition-metal ions with a 2,2′-bipyridyl alanine (bpyA) unit incorporated into the lactococcal multidrug resistance regulator (LmrR) scaffold is reported. The composition of the active site is shown to influence binding affinities. In the case of Fe(II), we demonstrate the need of additional ligating residues, in particular those containing carboxylate groups, in the vicinity of the binding site. Moreover, stabilization of di-tert-butylsemiquinone radical (DTB-SQ) in water was achieved by binding to the designed metalloproteins, which resulted in the radical being shielded from the aqueous environment. This allowed the first characterization of the radical semiquinone in water by resonance Raman spectroscopy.

UR - http://www.scopus.com/inward/record.url?scp=85033404257&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85033404257&partnerID=8YFLogxK

U2 - 10.1021/acs.inorgchem.7b02073

DO - 10.1021/acs.inorgchem.7b02073

M3 - Article

C2 - 29027794

AN - SCOPUS:85033404257

SN - 0020-1669

VL - 56

SP - 13293

EP - 13299

JO - Inorganic Chemistry

JF - Inorganic Chemistry

IS - 21

ER -

Artificial Metalloproteins for Binding and Stabilization of a Semiquinone Radical

Abstract

Funding

Access to Document

Persistent URL (handle)

Other files and links

Fingerprint

Cite this