The intriguing enhancement of chloroperoxidase mediated one-electron oxidations by azide, a known active-site ligand
- Heme and Flavo Proteins Laboratory, 204 Center for Biomedical Research, VIT University, Vellore 632014, Tamil Nadu (India)
- School of Molecular and Cellular Biology, University of Illinois (U-C), 600, S. Mathews, Urbana, IL 61801 (United States)
Highlights: Black-Right-Pointing-Pointer Azide is a well known heme-enzyme active site ligand and inhibitor. Black-Right-Pointing-Pointer Herein, azide is reported to enhance a set of heme-enzyme mediated reactions. Black-Right-Pointing-Pointer This effect is disconnected from native enzyme-azide binding. Black-Right-Pointing-Pointer Azide could enhance heme-enzyme reactions via a newly proposed mechanism. Black-Right-Pointing-Pointer Azide contained in reagents could impact reaction outcomes in redox biochemistry. -- Abstract: Azide is a well-known inhibitor of heme-enzymes. Herein, we report the counter-intuitive observation that at some concentration regimes, incorporation of azide in the reaction medium enhances chloroperoxidase (CPO, a heme-enzyme) mediated one-electron abstractions from several substrates. A diffusible azidyl radical based mechanism is proposed for explaining the phenomenon. Further, it is projected that the finding could have significant impact on routine in situ or in vitro biochemistry studies involving heme-enzyme systems and azide.
- OSTI ID:
- 22207587
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 415, Issue 4; Other Information: Copyright (c) 2011 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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