Broad-line nuclear magnetic resonance studies of chloroperoxidase
| Autor: | R. J. Smith, Lowell P. Hager, Robert G. Bryant, Gary E. Krejcarek |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Electron nuclear double resonance
Binding Sites Magnetic Resonance Spectroscopy Coordination sphere Protein Conformation Substrate (chemistry) Nuclear magnetic resonance spectroscopy Hydrogen-Ion Concentration Biochemistry Chloride Ion Fluorides Kinetics chemistry.chemical_compound Crystallography Chlorides Peroxidases chemistry Atom medicine Mitosporic Fungi Heme Protein Binding medicine.drug |
| Zdroj: | Biochemistry. 15:2508-2511 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00657a002 |
| Popis: | Chloroperoxidase, a heme glycoprotein isolated from the mold Caldariomyces fumago, was studied by NMR relaxation techniques. Interaction of the chloride ion substrate with the enzyme may be analyzed as consisting of at least three contributions: a weak interaction with the iron atom, nonspecific anion-protein interactions, and a specific interaction generated at low pH. The data indicate that a specific interaction, which develops in parallel with enzyme activity at low pH, does not occur at the iron atom first coordination sphere site. The results are summarized in terms of an enzymatic mechanism not involving chloride ion coordination to the iron atom. |
| Databáze: | OpenAIRE |
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