Dimethyl sulfoxide reductase, Raman

Dimethyl sulfoxide reductases from both R. sphaeroides and R. capsulatus have been the subject of several x-ray studies [112-115], In addition, extensive resonance Raman (RR) [119,125] and EXAFS studies [126,127] of both oxidized and reduced enzymes have been reported. Despite these studies, there is no single fully accepted picture for the active site of dmso reductase and its transformations during turnover. The following discussion outlines the structural features of the active site and the cofactor that are common to the various analyses as well as the current points of contention. 

Numerous oxo-molybdo-bis(dithiolene) and oxo-tungsto-bis(dithiolene) complexes have been synthesized and characterized as potential structural analogues of the active sites of the dimethyl sulfoxide reductase (DMSOR) and aldehyde oxidoreductase (AOR) families of mononuclear Mo and W enzymes [see Fig. 16 and Chapter 10 in this volume (50)]. The available IR and Raman data for the Mo and W complexes are summarized in Tables VII and VIII,... 

Garton, S. D., Hilton, J., Oku, H., Crouse, B. R., Rajagopalan, K. V., and Johnson, M. K., 1997, Active site structures and catalytic mechanism of Rhodobacter sphaeroides dimethyl sulfoxide reductase as revealed by resonance Raman spectroscopy, J. Am. Chem. Soc. 119 129061112916. 

Raman spectra have been reported for fullerene-like and nanotube MS2 (M = Mo or W) material. Resonance Raman spectra of four redox variants of Rhodobacter sphaeroides dimethyl sulfoxide reductase all contain vMoS of an... 

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