Elucidating and quantifying the importance of hydrogen bonding interactions in chemistry at metal sites

J C Mareque-Rivas, R T M de Rosales, E Salvagni, L Metteau, Rafael Torres Martin De Rosales

Research output: Contribution to journalMeeting abstractpeer-review

Abstract

The importance of the ligand environment in determining chemistry at metal sites is well understood. As a result, the vast majority of ligand designs in enzyme modelling chemistry are aimed at tuning metal chemistry through rational selection of coordinating groups. In Nature, however, it is known that the microenvironment of the active site can also influence the function of metalloproteins through non-covalent interactions such as H-bonding. In order to elucidate this aspect of enzyme catalysis we have been exploring the effects of H-bond donors on substrate binding, and chemical properties relevant to hydrolysis and redox chemistry at the metal site(s). Metal complexes of ligands with a range of H-bonding groups displaying internal H-bonds with other metal-bound ligands will be presented. The chemical effects exerted by these groups will be discussed, as will potential applications. The magnitudes of some beneficial effects caused by the H-bonding microenvironments will be compared with those ‘traditionally’ obtained by manipulating the primary coordination sphere.
Original languageEnglish
Pages (from-to)U777-U777
Number of pages1
JournalABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
Volume228
Publication statusPublished - 22 Aug 2004

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