Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
10.1126/science.272.5268.1615
Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and global climate regulation. The crystal structure of DMSO reductase from Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser 147 coordinates the metal in both states. The change in pterin coordination between the Mo(VI) and Mo(IV) forms suggests a mechanism for substrate binding and reduction by this enzyme. Sequence comparisons of DMSO reductase with a family of bacterial oxotransferases containing molybdopterin guanine dinucleotide indicate a similar polypeptide fold and active site with two molybdopterins within this family.

Bibliography

Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K. V., & Rees, D. C. (1996). Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination. Science, 272(5268), 1615–1621.

Authors 5
  1. Hermann Schindelin (first)
  2. Caroline Kisker (additional)
  3. James Hilton (additional)
  4. K. V. Rajagopalan (additional)
  5. Douglas C. Rees (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 27, 2006, 2:30 p.m.)
Deposited 1 year, 7 months ago (Jan. 12, 2024, 9:49 p.m.)
Indexed 3 weeks, 6 days ago (Aug. 2, 2025, 12:58 a.m.)
Issued 29 years, 2 months ago (June 14, 1996)
Published 29 years, 2 months ago (June 14, 1996)
Published Print 29 years, 2 months ago (June 14, 1996)
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@article{Schindelin_1996, title={Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination}, volume={272}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.272.5268.1615}, DOI={10.1126/science.272.5268.1615}, number={5268}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Schindelin, Hermann and Kisker, Caroline and Hilton, James and Rajagopalan, K. V. and Rees, Douglas C.}, year={1996}, month=jun, pages={1615–1621} }