Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 19, Issue 23, Pages 6709-6712Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2009.09.119
Keywords
Antibiotic; Cobalt; Copper; Catechol; EPR; Histatin; Metallopeptide; NMR; Oxidation
Categories
Funding
- National Science Foundation [CHE- 0718625]
- National High Magnetic Field Laboratory
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Histatin-5 (Hn5) is an antimicrobial salivary peptide of 24 amino acids. Two specific metal-binding sites were revealed with electronic, NMR, and EPR spectroscopy. The complex Cu-2(II)-Hn5 effectively oxidizes catechol, exhibiting enzyme-like kinetics (k(cat) = 0.011 and 0.060 s(1) and k(cat)/K-m = 19 and 50 M-1 s(1) without and with 12.8 mM H2O2, respectively). The significant oxidative activity may contribute to the biological activity of this antibiotic metallopeptide. (C) 2009 Elsevier Ltd. All rights reserved.
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