Re(CO)3(H2O)3+ binding to lysozyme: structure and reactivity

Sarah L. Binkley; Thomas C. Leeper; Roger S. Rowlett; Richard S. Herrick; Christopher J. Ziegler

doi:10.1039/C1MT00065A

Re(CO)₃(H₂O)₃⁺ binding to lysozyme: structure and reactivity

Sarah L. Binkley,^a Thomas C. Leeper,*^a Roger S. Rowlett,^b Richard S. Herrick^c and Christopher J. Ziegler*^a

* Corresponding authors

^a Department of Chemistry, University of Akron, Akron OH 44325-3601, USA
E-mail: tleeper@uakron.edu, ziegler@uakron.edu

^b Department of Chemistry, College of the Holy Cross, Worcester, USA
E-mail: rherrick@holycross.edu

^c Department of Chemistry, Colgate University, 13 Oak Drive, Hamilton, USA
E-mail: rrowlett@colgate.edu

Abstract

The reaction of Re(CO)₃(H₂O)₃⁺ with hen egg white lysozyme in aqueous solution results in a single covalent adduct. Both NMR spectroscopy and single crystal X-ray diffraction show that the rhenium tricarbonyl cation binds to His15via replacement of one of the coordinated water molecules. The formation of this adduct does not greatly affect the structure of the protein.

Metallomics

Re(CO)₃(H₂O)₃⁺ binding to lysozyme: structure and reactivity

Abstract

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