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Structures of the Superoxide Reductase from Pyrococcus furiosus in the Oxidized and Reduced States

Yeh, Andrew P. and Hu, Yonglin and Jenney, Francis E., Jr. and Adams, Michael W. W. and Rees, Douglas C. (2000) Structures of the Superoxide Reductase from Pyrococcus furiosus in the Oxidized and Reduced States. Biochemistry, 39 (10). pp. 2499-2508. ISSN 0006-2960. http://resolver.caltech.edu/CaltechAUTHORS:20150108-154842858

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Abstract

Superoxide reductase (SOR) is a blue non-heme iron protein that functions in anaerobic microbes as a defense mechanism against reactive oxygen species by catalyzing the reduction of superoxide to hydrogen peroxide [Jenney, F. E., Jr., Verhagen, M. F. J. M., Cui, X., and Adams, M. W. W. (1999) Science 286, 306−309]. Crystal structures of SOR from the hyperthermophilic archaeon Pyrococcus furiosus have been determined in the oxidized and reduced forms to resolutions of 1.7 and 2.0 Å, respectively. SOR forms a homotetramer, with each subunit adopting an immunoglobulin-like β-barrel fold that coordinates a mononuclear, non-heme iron center. The protein fold and metal center are similar to those observed previously for the homologous protein desulfoferrodoxin from Desulfovibrio desulfuricans [Coelho, A. V., Matias, P., Fülöp, V., Thompson, A., Gonzalez, A., and Carrondo, M. A. (1997) J. Bioinorg. Chem. 2, 680−689]. Each iron is coordinated to imidazole nitrogens of four histidines in a planar arrangement, with a cysteine ligand occupying an axial position normal to this plane. In two of the subunits of the oxidized structure, a glutamate carboxylate serves as the sixth ligand to form an overall six-coordinate, octahedral coordinate environment. In the remaining two subunits, the sixth coordination site is either vacant or occupied by solvent molecules. The iron centers in all four subunits of the reduced structure exhibit pentacoordination. The structures of the oxidized and reduced forms of SOR suggest a mechanism by which superoxide accessibility may be controlled and define a possible binding site for rubredoxin, the likely physiological electron donor to SOR.


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http://dx.doi.org/10.1021/bi992428k DOIArticle
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Contact Email Address:phoebe@caltech.edu
Additional Information:© 2000 American Chemical Society. Received October 19, 1999; Revised Manuscript Received December 22, 1999. Publication Date (Web): February 16, 2000. This work was supported in part by grants from the Department of Energy (FG05-95ER20175) and the National Science Foundation (MCB 9809060) to M.W.W.A. and from the National Institutes of Health (GM45162) to D.C.R. A.P.Y. was supported in part by a National Science Foundation Graduate Research Fellowship. The protein crystallographic facility at the Stanford Synchrotron Radiation Laboratory (SSRL) is funded by the Department of Energy, Office of Basic Energy Sciences, the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the Department of Energy, Office of Biological and Environmental Research. We greatly appreciate the contributions of Caroline Kisker, Hong Li, Hermann Schindelin, and Xiao-Dong Su to the structure determination.
Funders:
Funding AgencyGrant Number
Department of Energy (DOE)FG05-95ER20175
NSFMCB 9809060
NIHGM45162
NSF Graduate Research FellowshipUNSPECIFIED
Record Number:CaltechAUTHORS:20150108-154842858
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20150108-154842858
Official Citation:Structures of the Superoxide Reductase from Pyrococcus furiosus in the Oxidized and Reduced States†,‡ Andrew P. Yeh, Yonglin Hu, Francis E. Jenney, Jr., Michael W. W. Adams, and Douglas C. Rees Biochemistry 2000 39 (10), 2499-2508
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ID Code:53416
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:14 Jan 2015 07:26
Last Modified:14 Jan 2015 07:26

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