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Silver metallation of hen egg white lysozyme: X-ray crystal structure and NMR studies.

ABSTRACT: The X-ray crystal structure, NMR binding studies, and enzyme activity of silver(I) metallated hen egg white lysozyme are presented. Primary bonding of silver is observed through His15 with secondary bonding interactions coming from nearby Arg14 and Asp87. A covalently bound nitrate completes a four coordinate binding pocket.

SUBMITTER: Panzner MJ

PROVIDER: S-EPMC3677188 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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Silver metallation of hen egg white lysozyme: X-ray crystal structure and NMR studies.

Panzner Matthew J MJ Bilinovich Stephanie M SM Youngs Wiley J WJ Leeper Thomas C TC

Chemical communications (Cambridge, England) 20111031 46

The X-ray crystal structure, NMR binding studies, and enzyme activity of silver(I) metallated hen egg white lysozyme are presented. Primary bonding of silver is observed through His15 with secondary bonding interactions coming from nearby Arg14 and Asp87. A covalently bound nitrate completes a four coordinate binding pocket. ...[more]

PMID: 22042312

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