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Metal–thiolate bonds in bioinorganic chemistry
Author(s) -
Solomon Edward I.,
Gorelsky Serge I.,
Dey Abhishek
Publication year - 2006
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20451
Subject(s) - ionic bonding , chemistry , covalent bond , crystallography , chemical bond , bioinorganic chemistry , metal , pi bond , ligand (biochemistry) , hydrogen bond , electron transfer , redox , molecular orbital , bond order , inorganic chemistry , computational chemistry , ion , bond length , photochemistry , molecule , stereochemistry , crystal structure , organic chemistry , biochemistry , receptor
Metal–thiolate active sites play major roles in bioinorganic chemistry. The MS thiolate bonds can be very covalent, and involve different orbital interactions. Spectroscopic features of these active sites (intense, low‐energy charge transfer transitions) reflect the high covalency of the MS thiolate bonds. The energy of the metal–thiolate bond is fairly insensitive to its ionic/covalent and π/σ nature as increasing MS 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 cupric– and 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. J Comput Chem 27: 1415–1428, 2006