Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
- California Institute of Technology, Pasadena, CA (United States)
- Duke Univ., Durham, NC (United States)
The molybdoenzyme dimethysulfoxide (DMSO) reductase contributes to the release of dimethysulfide, 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{sup 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. 51 refs., 7 figs., 1 tab.
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 426163
- Journal Information:
- Science, Journal Name: Science Journal Issue: 5268 Vol. 272; ISSN SCIEAS; ISSN 0036-8075
- Country of Publication:
- United States
- Language:
- English
Similar Records
X-Ray Absorption Spectroscopic Characterization of the Molybdenum Site of 'Escherichia Coli' Dimethyl Sulfoxide Reductase
An X-ray spectroscopic investigation of bis(dithiolene)molybdenum(IV,V,VI) and -tungsten(IV,V,VI) complexes: Symmetrized structural representations of the active sites of molybdoenzymes in the DMSO reductase family and of tungstoenzymes in the AOR and F(M)DH families
Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria
Journal Article
·
Mon Jul 09 00:00:00 EDT 2007
· Inorg. Chem. 46:2,2007
·
OSTI ID:909799
An X-ray spectroscopic investigation of bis(dithiolene)molybdenum(IV,V,VI) and -tungsten(IV,V,VI) complexes: Symmetrized structural representations of the active sites of molybdoenzymes in the DMSO reductase family and of tungstoenzymes in the AOR and F(M)DH families
Journal Article
·
Tue Nov 09 23:00:00 EST 1999
· Journal of the American Chemical Society
·
OSTI ID:20013685
Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria
Journal Article
·
Tue Jan 31 23:00:00 EST 1984
· J. Bacteriol.; (United States)
·
OSTI ID:6265237