Protein crystal structures with ferrocene and ruthenocene-based enzyme inhibitors
Author(s) -
Adam J. Salmon,
Michael L. Williams,
Andreas Hofmann,
SallyAnn Poulsen
Publication year - 2012
Publication title -
chemical communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.837
H-Index - 333
eISSN - 1364-548X
pISSN - 1359-7345
DOI - 10.1039/c2cc15625c
Subject(s) - ruthenocene , ferrocene , carbonic anhydrase , chemistry , enzyme , active site , crystal structure , stereochemistry , combinatorial chemistry , crystallography , biochemistry , electrochemistry , electrode
We have determined the protein X-ray crystal structures of four organometallic inhibitors in complex with their target enzyme carbonic anhydrase II. The barrel-shaped hydrophobic ferrocene and ruthenocene moieties have provided a structure-based avenue to better occupy the hydrophobic binding patch within the enzyme active site.
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