Mossbauer and Electron Paramagnetic Resonance Studies of Chloroperoxidase Following Mechanism-Based Inactivation with Allylbenzene

We have used Mossbauer and electron paramagnetic resonance (EPR) spectroscopy to study a heme-N-alkylated derivative of chloroperoxidase (CPO) prepared by mechanism-based inactivation with allylbenzene and hydrogen peroxide. The freshly prepared inactivated enzyme (``green CPO'') displayed...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1996-11, Vol.93 (23), p.12791-12798
Hauptverfasser:	Debrunner, Peter G., Dexter, Annette F., Schulz, Charles E., Xia, Yao-Min, Hager, Lowell P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Allyl Compounds - pharmacology Benzene Derivatives - pharmacology Biochemistry Biological Sciences Chloride Peroxidase - antagonists & inhibitors Chloride Peroxidase - chemistry Chloride Peroxidase - isolation & purification Crystal field theory Electron Spin Resonance Spectroscopy Enzyme Inhibitors - pharmacology Enzymes Hydrogen peroxide Hydrogen Peroxide - pharmacology Inactivation Ligands Magnetic fields Mitosporic Fungi - enzymology Modeling Porphyrins Pyrroles Quadrupoles Resonance Spectroscopy, Mossbauer Tensors
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