Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination

Schindelin, Hermann; Kisker, Caroline; Hilton, J.; Rajagopalan, K.V.; Rees, Douglas C.

doi:10.1126/science.272.5268.1615

Cited by 467 publications

(561 citation statements)

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“…In 1996 X-ray crystal structures of oxidized and reduced forms of dimethyl sulfoxide reductase (DMSOR) provided key structural details revealing the nature of Moco [13]. Consistent with proposals based on earlier spectroscopic studies, Moco from oxidized DMSOR comprised a single Mo atom coordinated by two dithiolene chelates and a single terminal oxo ligand.…”

Section: Introductionmentioning

confidence: 57%

Synthesis, characterization, and spectroscopy of model molybdopterin complexes

Burgmayer

Kim

Petit

et al. 2007

Journal of Inorganic Biochemistry

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The preparation and characterization of new model complexes for the molybdenum cofactor are reported. The new models are distinctive for the inclusion of pterin-substituted dithiolene chelates and have the formulation Tp*MoX(pterin-R-dithiolene) (Tp* = tris(3,5,-dimethylpyrazolyl)borate), X= O, S, R= aryl or −C(OH)(CH 3 ) 2 ). Syntheses of Mo(4+) and (5+) complexes of two pterin-dithiolene derivatives as both oxo and sulfido compounds, and improved syntheses for pterinyl alkynes and [Et 4 N][Tp*Mo IV (S)S 4 ] reagents are described. Characterization methods include electrospray ionization mass spectrometry, electrochemistry, infrared spectroscopy, electron paramagnetic resonance and magnetic circular dichroism. Cyclic voltammetry reveals that the Mo(5+/4+) reduction potential is intermediate between that for dithiolene with electron-withdrawing substituents and simple dithiolate chelates. Electron paramagnetic resonance and magnetic circular dichroism of Mo(5+) complexes where X = O, R = aryl indicates that the molybdenum environment in the new models is electronically similar to that in Tp*MoO(benzenedithiolate).

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Section: Introductionmentioning

confidence: 57%

Synthesis, characterization, and spectroscopy of model molybdopterin complexes

Burgmayer

Kim

Petit

et al. 2007

Journal of Inorganic Biochemistry

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“…The first crystal structure reported for a member of this family was DMSO reductase [15,16]. However, our knowledge about this family was greatly increased with the study of nitrate reductase, which catalyzes the reduction of nitrate to nitrite, and formate dehydrogenase, involved in the oxidation of formate to carbon dioxide.…”

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confidence: 99%

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

et al. 2004

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Molybdenum and tungsten are second-and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site.

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“…Me 2 SO reductase from Escherichia coli and Rhodobacter sphaeroides catalyzes the reduction of Me 2 SO to DMS (7)(8)(9). This enzyme, which contains a molybdenum cofactor at the active center, is well characterized at the biochemical, biophysical, and molecular level and provides an excellent model system for investigating the structure and mechanism of electron transfer chain complexes (1,10). Saccharomyces cerevisiae has a number of NADPH-dependent enzymes that, in conjunction with methionine sulfoxide reductase (MXR1), can reduce Me 2 SO to DMS (11).…”

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confidence: 99%

Dimethyl Sulfoxide Exposure Facilitates Phospholipid Biosynthesis and Cellular Membrane Proliferation in Yeast Cells

Murata¹,

Watanabe²,

Sato³

et al. 2003

Journal of Biological Chemistry

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Me 2 SO is a polar solvent that is widely used in biochemistry, pharmacology, and industry. Although there are several reports in the literature concerning the biological effects of Me 2 SO, the total cellular response remains unclear. In this paper, DNA microarray technology combined with the hierarchical clustering bioinformatics tool was used to assess the effects of Me 2 SO on yeast cells. We found that yeast exposed to Me 2 SO increased phospholipid biosynthesis through up-regulated gene expression. It was confirmed by Northern blotting that the level of INO1 and OPI3 gene transcripts, encoding key enzymes in phospholipid biosynthesis, were significantly elevated following treatment with Me 2 SO. Furthermore, the phospholipid content of the cells increased during exposure to Me 2 SO as shown by conspicuous incorporation of a lipophilic fluorescent dye (3,3 -dihexyloxacarbocyanine iodide) into the cell membranes. From these results we propose that Me 2 SO treatment induces membrane proliferation in yeast cells to alleviate the adverse affects of this chemical on membrane integrity.Dimethyl sulfoxide (Me 2 SO) 1 is widely used as a solvent in the chemical industry and as a cryoprotectant in biotechnology. It is present in the environment as a waste product of the paper industry and from the production of dimethyl sulfide (DMS) and also arises from the degradation of sulfur-containing pesticides (1). In addition, Me 2 SO forms naturally from photooxidation of DMS in the atmosphere and from degradation of DMS by phytoplankton in the marine environment (2). Because Me 2 SO has low volatility and is highly hygroscopic, it is rapidly scavenged from the atmosphere by rain and returned to earth, and thereby plays a role in the global sulfur cycle (1, 3).Microorganisms, including both prokaryotes and eukaryotes, have the capability of reducing Me 2 SO and can utilize it as a terminal electron acceptor during anaerobic growth (4 -6). Me 2 SO reductase from Escherichia coli and Rhodobacter sphaeroides catalyzes the reduction of Me 2 SO to DMS (7-9). This enzyme, which contains a molybdenum cofactor at the active center, is well characterized at the biochemical, biophysical, and molecular level and provides an excellent model system for investigating the structure and mechanism of electron transfer chain complexes (1, 10). Saccharomyces cerevisiae has a number of NADPH-dependent enzymes that, in conjunction with methionine sulfoxide reductase (MXR1), can reduce Me 2 SO to DMS (11).In E. coli, the combination of divalent cations as Ca 2ϩ and Me 2 SO has been shown to stimulate the efficiency of DNA transfer into the cell (12). In the case of mammalian cells, it is reported that the transfection efficiency is increased by Me 2 SO treatment after electroporation (13). The exact mechanism of how Me 2 SO increases membrane permeability leading to DNA uptake is unclear.In mammalian cells Me 2 SO (2% (v/v)) can induce morphological changes, for example in mouse erythroleukemic cells (14), or cause differentiation, for example ...

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Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination

Cited by 467 publications

References 48 publications

Synthesis, characterization, and spectroscopy of model molybdopterin complexes

Synthesis, characterization, and spectroscopy of model molybdopterin complexes

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

Dimethyl Sulfoxide Exposure Facilitates Phospholipid Biosynthesis and Cellular Membrane Proliferation in Yeast Cells

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