Redox active motifs in selenoproteins

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 19, 2014, Pages 6976-6981

  Li, Fei ^a   Lutz, Patricia B ^b   Pepelyayeva, Yuliya ^a   Arnér, Elias S J ^c   Bayse, Craig A ^b   Rozovsky, Sharon ^a  

^a UNIVERSITY OF DELAWARE   (United States)

^b OLD DOMINION UNIVERSITY   (United States)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; CARBON; DIPHENYL DISELENIDE; RADIOPHARMACEUTICAL AGENT; SELENOPROTEIN; SELENOPROTEIN SELENIUM 77; UNCLASSIFIED DRUG;

ARTICLE; CALCULATION; CONTROLLED STUDY; DENSITY FUNCTIONAL THEORY; DISULFIDE BOND; DRUG PURIFICATION; ELECTROSPRAY; HUMAN; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SCANNER; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOPHILICITY; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTON NUCLEAR MAGNETIC RESONANCE; WASTE;

ANIMALS; BASE SEQUENCE; CATALYTIC DOMAIN; ESCHERICHIA COLI; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; SELENIUM; SELENOCYSTEINE; SELENOPROTEINS; SULFIDES; SULFUR; THERMODYNAMICS;

EID: 84900473347     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1319022111     Document Type: Article

References (36)

1. Rayman MP (2012) Selenium and human health. Lancet 379(9822):1256-1268.
2. Hatfield DL, Tsuji PA, Carlson BA, Gladyshev VN (2014) Selenium and selenocysteine: Roles in cancer, health, and development. Trends Biochem Sci 39(3):112-120.
3. Hondal RJ, Marino SM, Gladyshev VN (2013) Selenocysteine in thiol/disulfide-like exchange reactions. Antioxid Redox Signal 18(13):1675-1689.
4. Lu J, Holmgren A (2009) Selenoproteins. J Biol Chem 284(2):723-727.
5. Arnér ESJ (2010) Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine? Exp Cell Res 316(8):1296-1303.
6. Arnér ESJ (2009) Focus on mammalian thioredoxin reductases-important seleno-proteins with versatile functions. Biochim Biophys Acta 1790(6):495-526.
7. Gromer S, et al. (2003) Active sites of thioredoxin reductases: Why selenoproteins? Proc Natl Acad Sci USA 100(22):12618-12623.
8. Eckenroth BE, Lacey BM, Lothrop AP, Harris KM, Hondal RJ (2007) Investigation of the C-terminal redox center of high-Mr thioredoxin reductase by protein engineering and semisynthesis. Biochemistry 46(33):9472-9483.
9. Johansson L, Arscott LD, Ballou DP, Williams CH, Jr., Arnér ESJ (2006) Studies of an active site mutant of the selenoprotein thioredoxin reductase: The Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme. Free Radic Biol Med 41(4):649-656.
10. Hondal RJ (2009) Using chemical approaches to study selenoproteins-focus on thio-redoxin reductases. Biochim Biophys Acta 1790(11):1501-1512.
11. Ruggles EL, Deker PB, Hondal RJ (2009) Synthesis, redox properties, and conforma-tional analysis of vicinal disulfide ring mimics. Tetrahedron 65(7):1257-1267.
12. Hondal RJ, Ruggles EL (2011) Differing views of the role of selenium in thioredoxin reductase. Amino Acids 41(1):73-89.
13. Kryukov GV, et al. (2003) Characterization of mammalian selenoproteomes. Science 300(5624):1439-1443.
14. Arnér ESJ, Sarioglu H, Lottspeich F, Holmgren A, Böck A (1999) High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes. J Mol Biol 292(5):1003-1016.
15. Wessjohann LA, Schneider A, Abbas M, Brandt W (2007) Selenium in chemistry and biochemistry in comparison to sulfur. Biol Chem 388(10):997-1006.
16. Lillig CH, Holmgren A (2007) Thioredoxin and related molecules-from biology to health and disease. Antioxid Redox Signal 9(1):25-47.
17. 77Se-labeled ovine erythro-cyte glutathione peroxidase. J Biol Chem 266(8):4804-4809.
18. 77 NMR-spectroscopy. J Am Chem Soc 114(22):8573-8579.
19. 77Se NMR spectroscopy. Angew Chem 50(50):11952-11955.
20. 77Se enrichment of proteins expands the biological NMR toolbox. J Mol Biol 425(2):222-231.
21. 77Se chemical shift as a probe of selenium state in selenoproteins and their mimics. Inorg Chem 43(4):1208-1210.
22. 77 chemical shifts. J Chem Theory Comput 1(6):1119-1127.
23. 77Se NMR spectroscopy of selenoproteins. Biochalcogen Chemistry: The Biological Chemistry of Sulfur, Selenium, and Tellurium, eds Bayse CA, Brumaghim JL (Am Chem Soc, Washington, DC), pp 127-142.
24. Metanis N, Keinan E, Dawson PE (2006) Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency. J Am Chem Soc 128(51):16684-16691.
25. Liu J, Li F, Rozovsky S (2013) The intrinsically disordered membrane protein seleno-protein S is a reductase in vitro. Biochemistry 52(18):3051-3061.
26. Cenas N, et al. (2004) Interactions of quinones with thioredoxin reductase: A challenge to the antioxidant role of the mammalian selenoprotein. J Biol Chem 279(4): 2583-2592.
27. Johansson L, Gafvelin G, Arnér ESJ (2005) Selenocysteine in proteins-properties and biotechnological use. Biochim Biophys Acta 1726(1):1-13.
28. Cheng Q, Sandalova T, Lindqvist Y, Arnér ESJ (2009) Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1. J Biol Chem 284(6):3998-4008.
29. Creighton CJ, Reynolds CH, Lee DHS, Leo GC, Reitz AB (2001) Conformational analysis of the eight-membered ring of the oxidized cysteinyl-cysteine unit implicated in nicotinic acetylcholine receptor ligand recognition. J Am Chem Soc 123(50):12664-12669.
30. Hudáky I, et al. (2004) Vicinal disulfide bridge conformers by experimental methods and by ab initio and DFT molecular computations. Proteins 55(1):152-168.
31. Jeng MF, Holmgren A, Dyson HJ (1995) Proton sharing between cysteine thiols in Escherichia coli thioredoxin: Implications for the mechanism of protein disulfide reduction. Biochemistry 34(32):10101-10105.
32. Avizonis DZ, FarrJones S, Kosen PA, Basus VJ (1996) Conformations and dynamics of the essential cysteinyl-cysteine ring derived from the acetylcholine receptor. J Am Chem Soc 118(51):13031-13039.
33. Frisch MJ, et al. (2009) Gaussian 09 (Gaussian, Wallingford, CT).
34. Dunning TH (1971) Gaussian basis functions for use in molecular calculations. 3. Contraction of (10S6P) atomic basis sets for first-row atoms. J Chem Phys 55(2): 716-723.
35. Wadt WR, Hay PJ (1985) ab initio effective core potentials for molecular calculations-potentials for main group elements Na to Bi. J Chem Phys 82(1):284-298.
36. Hurley MM, Pacios LF, Christiansen PA, Ross RB, Ermler WC (1986) ab initio relativistic effective potentials with spin-orbit operators. 2. K through Kr. J Chem Phys 84(12): 6840-6853.