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Dimethyl sulfoxide reductase

Wan J, TK Tokunaga, E Brodie, Z Wang, Z Zheng, D Herman, TC Hazen, MK Firestone, SR Sutton (2005) Reoxidation of bioreduced uranium under reducing conditions. Environ Sci Technol 39 6162-6169. Weiner JH, DP Macisaac, RE Bishop, PT Bilous (1988) Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity J Bacterial 170 1505-1510. [Pg.162]

McEwan AG, Benson N, BonnetTC, et al. 1991. Bacterial dimethyl sulfoxide reductases and nitrate reductases. Biochem Soc Trans 19 605-8. [Pg.203]

Johnson, J.L., Bastian, N.R. Rajagopalan, K.V. (1990). Molybdop-terin guanine dinucleotide a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. Proceedings of the National Academy of Sciences (USA) 87, 3190-4. [Pg.72]

IV.C.2. The Active Site of Dimethyl Sulfoxide Reductase (R. sphaeroides and R. capsulatus)... [Pg.109]

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. [Pg.109]

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,... [Pg.241]

Dimethyl sulfoxide reductases (DMSOR) of bacteria and fungi that catalyze the reduction of DMSO to dimethyl sulfide (DMS). These enzymes play a significant role in the global sulfur cycle, not least because DMS is volatile and is the precursor of the methylsulfonate aerosols that nucleate cloud formation (29). Furthermore, the distinctive smell of DMS acts as a guide to certain seabirds who use it to locate productive regions of the ocean (30). [Pg.540]


See other pages where Dimethyl sulfoxide reductase is mentioned: [Pg.13]    [Pg.139]    [Pg.28]    [Pg.44]    [Pg.197]    [Pg.213]    [Pg.250]    [Pg.497]    [Pg.515]    [Pg.531]    [Pg.577]    [Pg.28]    [Pg.44]    [Pg.197]    [Pg.213]    [Pg.250]    [Pg.497]    [Pg.515]    [Pg.531]   
See also in sourсe #XX -- [ Pg.563 , Pg.564 , Pg.565 , Pg.566 , Pg.567 , Pg.568 ]

See also in sourсe #XX -- [ Pg.563 , Pg.564 , Pg.565 , Pg.566 , Pg.567 , Pg.568 ]




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Dimethyl sulfoxide reductase active site structure

Dimethyl sulfoxide reductase family

Dimethyl sulfoxide reductase molybdenum enzymes

Dimethyl sulfoxide reductase, Raman

Pyranopterin dithiolenes dimethyl sulfoxide reductase

Sulfoxides dimethyl

Sulfoxides dimethyl sulfoxide

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