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Post-Protein-Binding Reactivity and Modifications of the fac-Re(CO)(3)](+) Core


Zobi, Fabio; Spingler, Bernhard (2012). Post-Protein-Binding Reactivity and Modifications of the fac-Re(CO)(3)](+) Core. Inorganic Chemistry, 51(3):1210-1212.

Abstract

The reactivity of the Re(CO)(3)(H2O)(2)](+) complex coordinated to the His15 residue of HEW lysozyme is described. In the fully metalated protein (Lys-1), the Re ion retains its reactivity only toward selected ligands, while others induce a ligand-mediated demetalation of the enzyme. It is further shown that some of the complexes that may be ``engineered'' on the lysozyme do not react with the free protein even if present in solution in excess. The formation of stable metal adducts starting from Lys-1 was confirmed by X-ray crystallography.

The reactivity of the Re(CO)(3)(H2O)(2)](+) complex coordinated to the His15 residue of HEW lysozyme is described. In the fully metalated protein (Lys-1), the Re ion retains its reactivity only toward selected ligands, while others induce a ligand-mediated demetalation of the enzyme. It is further shown that some of the complexes that may be ``engineered'' on the lysozyme do not react with the free protein even if present in solution in excess. The formation of stable metal adducts starting from Lys-1 was confirmed by X-ray crystallography.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:February 2012
Deposited On:17 Oct 2012 12:36
Last Modified:05 Apr 2016 15:59
Publisher:American Chemical Society
ISSN:0020-1669
Additional Information:This document is the Accepted Manuscript version of a Published Work that appeared in final form in Inorganic Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher.
Publisher DOI:https://doi.org/10.1021/ic2023314
Other Identification Number:ISI:000300474700004
Permanent URL: https://doi.org/10.5167/uzh-65334

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