Metal-thiolate bonds in bioinorganic chemistry

Abstract

Metal-thiolate active sites play major roles in bioinorganic chemistry. The M-S thiolate bonds can be very covalent, and involve different orbital interactions. Spectroscopic features of these active sites (intense, lowenergy charge transfer transitions) reflect the high covalency of the M-S thiolate bonds. The energy of the metal-thiolate bond is fairly insensitive to its ionic/covalent and π/σ nature as increasing M-S covalency reduces the charge distribution, hence the ionic term, and these contributions can compensate. Thus, trends observed in stability constants (i.e., the Irving-Williams series) mostly reflect the dominantly ionic contribution to bonding of the innocent ligand being replaced by the thiolate. Due to high effective nuclear charges of the Cu II and Fe III ions, the cupricand ferric-thiolate bonds are very covalent, with the former having strong π and the latter having more σ character. For the blue copper site, the high π covalency couples the metal ion into the protein for rapid directional long range electron transfer. For rubredoxins, because the redox active molecular orbital is π in nature, electron transfer tends to be more localized in the vicinity of the active site. Although the energy of hydrogen bonding of the protein environment to the thiolate ligands tends to be fairly small, H-bonding can significantly affect the covalency of the metal-thiolate bond and contribute to redox tuning by the protein environment. © 2006 Wiley Periodicals, Inc.