Log InRegister
Quick Links : The Mindat ManualThe Rock H. Currier Digital LibraryMindat Newsletter [Free Download]
Home PageAbout MindatThe Mindat ManualHistory of MindatCopyright StatusWho We AreContact UsAdvertise on Mindat
Donate to MindatCorporate SponsorshipSponsor a PageSponsored PagesMindat AdvertisersAdvertise on Mindat
Learning CenterWhat is a mineral?The most common minerals on earthInformation for EducatorsMindat ArticlesThe ElementsThe Rock H. Currier Digital LibraryGeologic Time
Minerals by PropertiesMinerals by ChemistryAdvanced Locality SearchRandom MineralRandom LocalitySearch by minIDLocalities Near MeSearch ArticlesSearch GlossaryMore Search Options
Search For:
Mineral Name:
Locality Name:
Keyword(s):
 
The Mindat ManualAdd a New PhotoRate PhotosLocality Edit ReportCoordinate Completion ReportAdd Glossary Item
Mining CompaniesStatisticsUsersMineral MuseumsClubs & OrganizationsMineral Shows & EventsThe Mindat DirectoryDevice SettingsThe Mineral Quiz
Photo SearchPhoto GalleriesSearch by ColorNew Photos TodayNew Photos YesterdayMembers' Photo GalleriesPast Photo of the Day GalleryPhotography

Zhong, L., Arner, E. S. J., Holmgren, A. (2000) Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proceedings of the National Academy of Sciences, 97 (11) 5854-5859 doi:10.1073/pnas.100114897

Advanced
   -   Only viewable:
Reference TypeJournal (article/letter/editorial)
TitleStructure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
JournalProceedings of the National Academy of Sciences
AuthorsZhong, L.Author
Arner, E. S. J.Author
Holmgren, A.Author
Year2000 (May 23)Volume97
Issue11
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.100114897Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1640306Long-form Identifiermindat:1:5:1640306:2
GUID0
Full ReferenceZhong, L., Arner, E. S. J., Holmgren, A. (2000) Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proceedings of the National Academy of Sciences, 97 (11) 5854-5859 doi:10.1073/pnas.100114897
Plain TextZhong, L., Arner, E. S. J., Holmgren, A. (2000) Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proceedings of the National Academy of Sciences, 97 (11) 5854-5859 doi:10.1073/pnas.100114897
In(2000, May) Proceedings of the National Academy of Sciences Vol. 97 (11) Proceedings of the National Academy of Sciences

See Also

These are possibly similar items as determined by title/reference text matching only.

Lee, S.-R., Bar-Noy, S., Kwon, J., Levine, R. L., Stadtman, T. C., Rhee, S. G. (2000) Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity. Proceedings of the National Academy of Sciences, 97 (6) 2521-2526 doi:10.1073/pnas.050579797
Sandalova, T., Zhong, L., Lindqvist, Y., Holmgren, A., Schneider, G. (2001) Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme. Proceedings of the National Academy of Sciences, 98 (17) 9533-9538 doi:10.1073/pnas.171178698
Pader, I., Sengupta, R., Cebula, M., Xu, J., Lundberg, J. O., Holmgren, A., Johansson, K., Arner, E. S. J. (2014) Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase. Proceedings of the National Academy of Sciences, 111 (19) 6964-6969 doi:10.1073/pnas.1317320111
Lu, J., Chew, E.-H., Holmgren, A. (2007) Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proceedings of the National Academy of Sciences, 104 (30) 12288-12293 doi:10.1073/pnas.0701549104
Holmgren, A., Lyckeborg, C. (1980) Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase. Proceedings of the National Academy of Sciences, 77 (9) 5149-5152 doi:10.1073/pnas.77.9.5149
Arscott, L. D., Gromer, S., Schirmer, R. H., Becker, K., Williams, C. H. (1997) The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Proceedings of the National Academy of Sciences, 94 (8) 3621-3626 doi:10.1073/pnas.94.8.3621
Patel, P. H., Loeb, L. A. (2000) DNA polymerase active site is highly mutable: Evolutionary consequences. Proceedings of the National Academy of Sciences, 97 (10) 5095-5100 doi:10.1073/pnas.97.10.5095
Li, F., Lutz, P. B., Pepelyayeva, Y., Arner, E. S. J., Bayse, C. A., Rozovsky, S. (2014) Redox active motifs in selenoproteins. Proceedings of the National Academy of Sciences, 111 (19) 6976-6981 doi:10.1073/pnas.1319022111
Gromer, S., Johansson, L., Bauer, H., Arscott, L. D., Rauch, S., Ballou, D. P., Williams, C. H., Schirmer, R. H., Arner, E. S. J. (2003) Active sites of thioredoxin reductases: Why selenoproteins?. Proceedings of the National Academy of Sciences, 100 (22) 12618-12623 doi:10.1073/pnas.2134510100
Zhao, R., Masayasu, H., Holmgren, A. (2002) Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant. Proceedings of the National Academy of Sciences, 99 (13) 8579-8584 doi:10.1073/pnas.122061399
Mertz, E. L., Krishtalik, L. I. (2000) Low dielectric response in enzyme active site. Proceedings of the National Academy of Sciences, 97 (5) 2081-2086 doi:10.1073/pnas.050316997
 
and/or  
Mindat.org is an outreach project of the Hudson Institute of Mineralogy, a 501(c)(3) not-for-profit organization.
Copyright © mindat.org and the Hudson Institute of Mineralogy 1993-2025, except where stated. Most political location boundaries are Β© OpenStreetMap contributors. Mindat.org relies on the contributions of thousands of members and supporters. Founded in 2000 by Jolyon Ralph.
To cite: Ralph, J., Von Bargen, D., Martynov, P., Zhang, J., Que, X., Prabhu, A., Morrison, S. M., Li, W., Chen, W., & Ma, X. (2025). Mindat.org: The open access mineralogy database to accelerate data-intensive geoscience research. American Mineralogist, 110(6), 833–844. doi:10.2138/am-2024-9486.
Privacy Policy - Terms & Conditions - Contact Us / DMCA issues - Report a bug/vulnerability Current server date and time: August 26, 2025 16:07:51
Go to top of page