Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

Metallothioneins with unusual residues : histidines as modulators of zinc affinity and reactivity

Tools
- Tools
+ Tools

Blindauer, Claudia A. (2008) Metallothioneins with unusual residues : histidines as modulators of zinc affinity and reactivity. In: 1st Georgian Bay International Conference on Bioinorganic Chemistry, Parry Sound, Canada, 22-25 May 2007. Published in: Journal of Inorganic Biochemistry, Vol.102 (No.3). pp. 507-521.

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.jinorgbio.2007.10.032

Abstract

For many years, paradigms regarding metallothioneins comprised the exclusive metal coordination by thiolates from cysteine residues and the absence of aromatic residues. As more sequence and in vitro data on metallothioneins, in particular from non-vertebrate organisms, has become available, both the occurrence of and metal coordination by histidine residues in metallothioneins is emerging as a more frequent feature than expected. We discuss the general implications of histidines versus cysteines in zinc binding sites, and review some recent results from literature and our own lab. We conclude that histidines can stabilise metallothionein clusters by reducing the overall charge, offering the ability to help with structural organisation by supplying H-bond donor and acceptor properties, reducing the likelihood for disulfide bond formation, whilst maintaining a high affinity towards metal ions, in particular the borderline zinc ion. (C) 2007 Elsevier Inc. All rights reserved.

Item Type: Conference Item (Paper)
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Divisions: Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH): Zinc, Metallothionein, Bioinorganic chemistry, Amino acids
Journal or Publication Title: Journal of Inorganic Biochemistry
Publisher: Elsevier Science Inc
ISSN: 0162-0134
Date: March 2008
Volume: Vol.102
Number: No.3
Number of Pages: 15
Page Range: pp. 507-521
Identification Number: 10.1016/j.jinorgbio.2007.10.032
Status: Peer Reviewed
Publication Status: Published
Funder: Royal Society (Great Britain), Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung [Swiss National Science Foundation], Novartis Foundation, European Commission (EC), Wellcome Trust (London, England)
Conference Paper Type: Paper
Title of Event: 1st Georgian Bay International Conference on Bioinorganic Chemistry
Type of Event: Conference
Location of Event: Parry Sound, Canada
Date(s) of Event: 22-25 May 2007
URI: http://wrap.warwick.ac.uk/id/eprint/30326

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us