The MoOS₃ active site of sulfite oxidase has drawn attention to a relatively unexplored area of molybdenum coordination chemistry. Cis,trans-(L-N₂S₂)MoᵛO(SR)[L-N₂S₂H₂ = N,N '-dimethyl-N,N'-bis(mercaptophenyl)ethylenediamine: R = CH₂Ph. CH₂CH₃, and p-C₆H₄-Y (Y = CF₃, Cl, Br, F, H, CH₃, CH₂CH₃, and OCH₃)] are the first structurally, spectroscopically, and electrochemically characterized mononuclear Mo compounds with three thiolate donors in the equatorial, as occurs in sulfite oxidase. These compounds provide a well-defined platform for the systematic investigation of the electronic structures of the MoᵛOS₃ centers and their implications for molybdoenzymes. Single crystal electron paramagnetic resonance spectroscopy was used to study cis,trans-(L-N₂S₂)MoᵛOCl and determine the relationship between the molecular and magnetic structure. These studies furnish a better understanding of the CW-EPR parameters exhibited by the various Mo(V) forms of the mononuclear molybdenum enzymes.
| Identifer | oai:union.ndltd.org:arizona.edu/oai:arizona.openrepository.com:10150/284099 |
| Date | January 2000 |
| Creators | Mader, Michele Lynn |
| Contributors | Enemark, John H. |
| Publisher | The University of Arizona. |
| Source Sets | University of Arizona |
| Language | en_US |
| Detected Language | English |
| Type | text, Dissertation-Reproduction (electronic) |
| Rights | Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. |
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