Table of Contents
International Journal of Inorganic Chemistry
Volume 2011, Article ID 395418, 4 pages
Research Article

Improvement of Aminopeptidase Activity of Dizinc(II) Complexes by Increasing Substrate Accessibility

Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Kojirakawa, Yamagata 990-8560, Japan

Received 22 November 2010; Accepted 2 March 2011

Academic Editor: Rabindranath Mukherjee

Copyright © 2011 Md. Jamil Hossain et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


A new dizinc(II) complex, [Zn2(bhmp)(MeCO2)2]BPh4 [(bhmp): 2,6-bis[bis(2-hydroxyethyl)aminomethyl]-4-methylphenolate anion], performs aminopeptidase activity to hydrolyze L-leucine-p-nitroanilide. As compared with a related dizinc(II) complex [Zn2(bomp)(MeCO2)2]BPh4 [(bomp): 2,6-bis[bis(2-methoxyethyl)aminomethyl]-4-methylphenolate anion], the activity of the present bhmp complex was about 80 times greater than that of the bomp complex. This is mainly because the substrate accessibility was improved by changing the terminal methoxy groups to hydroxyl groups.