Biomimetic chemistry of iron, nickel, molybdenum, and tungsten in sulfur-ligated protein sites.
Biomimetic inorganic chemistry has as its primary goal the synthesis of molecules that approach or achieve the structures, oxidation states, and electronic and reactivity features of native metal-containing sites of variant nuclearity. Comparison of properties of accurate analogues and these sites ideally provides insight into the influence of protein structure and environment on intrinsic properties as represented by the analogue. For polynuclear sites in particular, the goal provides a formidable challenge for, with the exception of iron-sulfur clusters, all such site structures have never been achieved and few have even been closely approximated by chemical synthesis. This account describes the current status of the synthetic analogue approach as applied to the mononuclear sites in certain molybdoenzymes and the polynuclear sites in hydrogenases, nitrogenase, and carbon monoxide dehydrogenases.
Groysman
Stanislav
S
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Holm
R H
RH
D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D032701:Biomimetics; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D008982:Molybdenum / Q000737:chemistry*; D009532:Nickel / Q000737:chemistry*; D011485:Protein Binding; D014414:Tungsten / Q000737:chemistry*
D001426:Bacterial Proteins; D009532:Nickel; D008982:Molybdenum; D007501:Iron; D014414:Tungsten