Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1317063 | Journal of Inorganic Biochemistry | 2007 | 7 Pages |
Abstract
Molybdenum- or tungsten-containing enzymes catalyze oxygen atom transfer reactions involved in carbon, sulfur, or nitrogen metabolism. It has been observed that reduction potentials and oxygen atom transfer rates are different for W relative to Mo enzymes and the isostructural Mo/W complexes. Sulfur K-edge X-ray absorption spectroscopy (XAS) and density functional theory (DFT) calculations on [MoVO(bdt)2]− and [WVO(bdt)2]−, where bdt = benzene-1,2-dithiolate(2-), have been used to determine that the energies of the half-filled redox-active orbital, and thus the reduction potentials and MO bond strengths, are different for these complexes due to relativistic effects in the W sites.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Adam L. Tenderholt, Robert K. Szilagyi, Richard H. Holm, Keith O. Hodgson, Britt Hedman, Edward I. Solomon,