Issue 8, 2011
From the journal:

MedChemComm

Metal preference of Zn(ii) and Co(ii) for the dinuclear metal binding site of IMP-1 metallo-β-lactamase and spectroscopic properties of Co(ii)-substituted IMP-1 with mercaptoacetic acid†

Yoshihiro Yamaguchi,‡*a   Kayo Imamura,b   Ako Sasao,c   Emi Murakami,b   Yoshichika Arakawa§d  and  Hiromasa Kurosaki‡*b  

* Corresponding authors

a Environmental Safety Center, Kumamoto University, 39-1 Kurokami 2-Chome, Kumamoto, Japan
E-mail: yyamagu@gpo.kumamoto-u.ac.jp
Fax: +81 96 342 3237
Tel: +81 96 342 3238

b Department of Structure–Function Physical Chemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Kumamoto, Japan
E-mail: ayasaya@gpo.kumamoto-u.ac.jp
Fax: +81 96 371 4314
Tel: +81 96 371 4314

c Department of Forensic Medicine, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, Japan

d Department of Bacterial Pathogenesis and Infection Control, National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashi-Murayama, Tokyo, Japan

Abstract

IMP-1 metallo-β-lactamase is a dinuclear Zn(II) enzyme that catalyzes the hydrolysis and inactivation of most β-lactams including carbapenems, and is involved in one of the mechanisms for generating clinical resistance to antibiotics in pathogenic bacteria. We investigated the metal preferences of Zn(II) and Co(II) for the apo-enzyme of IMP-1 metallo-β-lactamase, apo-IMP-1, which contains a dinuclear metal binding site (the Zn1 and Zn2 sites), by UV-visible spectroscopy. The UV-visible spectrum of apo-IMP-1 containing 1 equiv. of Co(II) and 1 equiv. of Zn(II) showed a high preference of Zn(II) for the Zn1 site compared to Co(II). Moreover, Zn(II) bound more strongly to the Zn2 site than Co(II). The interaction of IMP-1 metallo-β-lactamase with mercaptoacetic acid was also investigated using Co(II)-substituted IMP-1 and UV-visible spectroscopy. Possible metal binding modes of Co(II) or Zn(II) to the dinuclear metal binding site in apo-IMP-1 and of mercaptoacetic acid to Co(II)-substituted IMP-1 are proposed.

Graphical abstract: Metal preference of Zn(ii) and Co(ii) for the dinuclear metal binding site of IMP-1 metallo-β-lactamase and spectroscopic properties of Co(ii)-substituted IMP-1 with mercaptoacetic acid

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Article information

DOI
https://doi.org/10.1039/C1MD00062D
Article type
Concise Article
Submitted
28 Feb 2011
Accepted
06 May 2011
First published
02 Jun 2011

Med. Chem. Commun., 2011,2, 720-725

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Metal preference of Zn(II) and Co(II) for the dinuclear metal binding site of IMP-1 metallo-β-lactamase and spectroscopic properties of Co(II)-substituted IMP-1 with mercaptoacetic acid

Y. Yamaguchi, K. Imamura, A. Sasao, E. Murakami, Y. Arakawa and H. Kurosaki, Med. Chem. Commun., 2011, 2, 720 DOI: 10.1039/C1MD00062D

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