Binuclear non-heme iron enzymes

Mitić, Nataša, Schenk, Gerhard and Hanson, Graeme R. (2009). Binuclear non-heme iron enzymes. In Graeme Hanson and Lawrence Berliner (Ed.), High resolution EPR: applications to metalloenzymes and metals in medicine (pp. 269-395) New York, NY, United States: Springer. doi:10.1007/978-0-387-84856-3_7

Author Mitić, Nataša
Schenk, Gerhard
Hanson, Graeme R.
Title of chapter Binuclear non-heme iron enzymes
Title of book High resolution EPR: applications to metalloenzymes and metals in medicine
Place of Publication New York, NY, United States
Publisher Springer
Publication Year 2009
Sub-type Research book chapter (original research)
DOI 10.1007/978-0-387-84856-3_7
Open Access Status
Series Biological Magnetic Resonance
ISBN 9780387848556
ISSN 0192-6020
Editor Graeme Hanson
Lawrence Berliner
Volume number 28
Chapter number 7
Start page 269
End page 395
Total pages 127
Total chapters 14
Collection year 2010
Language eng
Subjects 060107 Enzymes
970103 Expanding Knowledge in the Chemical Sciences
970106 Expanding Knowledge in the Biological Sciences
Formatted Abstract/Summary
Binuclear non-heme iron enzymes are a large group of enzymes that catalyze a variety of chemical reactions and are involved in numerous metabolic functions. In this review, the structural and biochemical properties of representatives of every class of this group of enzymes are described. The contributions of electron paramagnetic resonance-related techniques to our understanding of structure and reactivity of binuclear non-heme iron enzymes are discussed, and, where appropriate, supported by data obtained from complementary spectroscopic methods. This chapter is intended as a guide to illustrate the usefulness of electron paramagnetic resonance-related techniques in the study of these enzymes. Consequently, technical details were kept to a minimum.
© Springer Science+Business Media, LLC 2009
Q-Index Code B1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published in Part Two: "Iron Proteins".

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Created: Tue, 23 Feb 2010, 09:11:38 EST by Laura McTaggart on behalf of School of Chemistry & Molecular Biosciences