Molybdenum enzymes model

J. T. Bolin and co-workers, in E. I. Stiefel, D. Coucouvanis, and W. E. Newton, eds.. Molybdenum Enzymes, Cofaetors and Model Systems American... 

Stifel, E. L Coucouvanis, D. Newton, W. E., Eds. Molybdenum Enzymes, Cofactors and Model Systems, ACS Symposium Series 535 American Chemical Society Washington, DC, 1993 Chapters 10-23. 

Mononuclear Mov complexes with sterically hindered monodentate thiolato ligands are of interest as models for special molybdenum enzymes (the Mo oxidases). Here dimer formation via thiolato bridges and sulfide formation by C—S bond cleavage do not occur. Such a ligand is TIPTH. The complex [Mo(CO)2(TIPT)3) (14), with essentially trigonal prismatic coordination about Mo and trans CO groups in the axial sites, can be obtained.91... 

One important feature of Mov intermediate species during enzymatic reaction is the presence of superhyperfine splitting from a proton. Mov model compounds with coordinated N—H groups display superhyperfine coupling of the same order of magnitude as that found in molybdenum enzymes.1002... 

The most detailed spectroscopic and electronic structure studies of metallo-mono(dithiolenes) have focused on the nature of ligand-to-ligand charge transfer (LLCT) excitations in [M(diimine)(dithiolene)] complexes (112, 250-257, 262, 264, 295-301) and in monooxo molybdenum dithiolenes (19, 20, 22, 23) as models for pyranopterin molybdenum enzymes such as sulfite oxidase (SO). Since metallo-mono(dithiolenes) generally possess little or no symmetry, detailed spectrosopic and electronic structure studies of this class of metallo-dithiolenes have only recently begun to appear. The analysis of the spectroscopic data has been aided by the fact that the dithiolene-to-metal charge... 

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