CaltechAUTHORS
  A Caltech Library Service

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

Schindelin, Hermann and Kisker, Caroline and Hilton, James and Rajagopalan, K. V. and Rees, Douglas C. (1996) Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination. Science, 272 (5268). pp. 1615-1621. ISSN 0036-8075. https://resolver.caltech.edu/CaltechAUTHORS:20150113-144809357

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20150113-144809357

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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.272.5268.1615DOIArticle
http://www.sciencemag.org/content/272/5268/1615PublisherArticle
http://www.jstor.org/stable/2890668JSTORArticle
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 1996 American Association for the Advancement of Science. 15 January 1996: Accepted 23 April 1996. We thank J. Enemark for insightful discussions and suggestions on the manuscript. Supported by Deutsche Forschungsgemeinschaft postdoctoral fellowships (to C.K. and H.S.), by USPHS grant GM50775 (D.C.R.), and by USPHS grant GM00091 (K.V.R.). The rotation camera facility at SSRL is supported by the Department of Energy and NIH. The X-PLOR calculations were performed on the CRAY C90 at the San Diego Supercomputer Center, supported by the NSF. Coordinates have been deposited in the Brookhaven Protein Data Bank and can be supplied by e-mail to hermann@citray.caltech.edu.
Funders:
Funding AgencyGrant Number
Deutsche Forschungsgemeinschaft (DFG)UNSPECIFIED
USPHSGM50775
USPHSGM00091
Department of Energy (DOE)UNSPECIFIED
NIHUNSPECIFIED
NSFUNSPECIFIED
Issue or Number:5268
Record Number:CaltechAUTHORS:20150113-144809357
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150113-144809357
Official Citation: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. doi: 10.1126/science.272.5268.1615
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53637
Collection:CaltechAUTHORS
Deposited By: Joanne McCole
Deposited On:14 Jan 2015 00:11
Last Modified:03 Oct 2019 07:51

Repository Staff Only: item control page