Skip Nav Destination
Metallobiology
Heme Peroxidases
Edited by
Brian Dunford
Brian Dunford
University of Alberta, Canada
Search for other works by this author on:
Hardback ISBN:
978-1-84973-911-5
PDF ISBN:
978-1-78262-262-8
EPUB ISBN:
978-1-78262-742-5
No. of Pages:
366
Publication date:
26 Oct 2015
Book Chapter
Chapter 5: Heme Peroxidase Kinetics
By
H. Brian Dunford
H. Brian Dunford
Search for other works by this author on:
-
Published:26 Oct 2015
-
Citation
H. B. Dunford, in Heme Peroxidases, ed. E. Raven and B. Dunford, The Royal Society of Chemistry, 2015, ch. 5, pp. 99-112.
Download citation file:
One of the longest and most intensively studied enzymes is horseradish peroxidase. Its reactions are reviewed from historical, kinetic and mechanistic perspectives. Kinetics studies include steady state, transient state and relaxation kinetics. The methods and reasoning involved are applicable to other peroxidases and indeed to other enzymes. Accumulated evidence from several techniques indicate that distal His 42 plays a key role in its redox reactions. The possible implications of recent low temperature neutron diffraction experiments on oxidized yeast cytochrome c peroxidase are discussed.
You do not currently have access to this chapter, but see below options to check access via your institution or sign in to purchase.
Digital access
$64.60