Selenocysteine in proteins - Properties and biotechnological use

Biochimica et Biophysica Acta - General Subjects

Volumn 1726, Issue 1, 2005, Pages 1-13

  Johansson, Linda ^a   Gafvelin, Guro ^a   Arnér, Elias S J ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Biotechnology; Enzymology; Selenium biochemistry; Selenocysteine; Selenoprotein; Synthetic and recombinant selenoprotein production

Indexed keywords

CARBON 11; FLUORESCENT DYE; OXIDOREDUCTASE; RECOMBINANT PROTEIN; SELENOCYSTEINE; SELENOPROTEIN; THIOL;

AFFINITY LABELING; BIOTECHNOLOGY; CONJUGATION; ELECTROCHEMISTRY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME MECHANISM; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; GAMMA RADIATION; GENE INSERTION; GENETIC CODE; HUMAN; ISOTOPE LABELING; MOLECULAR PROBE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PHYSICAL CHEMISTRY; POSITRON; POSITRON EMISSION TOMOGRAPHY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; PROTEIN TARGETING; REVIEW; RIBOSOME; SELENIUM 77 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; X RAY CRYSTALLOGRAPHY;

BIOTECHNOLOGY; CODON; PROTEIN BINDING; PROTEINS; RIBOSOMES; SELENOCYSTEINE;

ESCHERICHIA COLI;

EID: 27144469008     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.05.010     Document Type: Review

References (121)

1. D.P. Gamblin, P. Garnier, S. van Kasteren, N.J. Oldham, A.J. Fairbanks, and B.G. Davis Glyco-SeS: selenenylsulfide-mediated protein glycoconjugation-A new strategy in post-translational modification Angew. Chem., Int. Ed. Engl. 43 2004 828 833
2. C. Jacob, G.I. Giles, N.M. Giles, and H. Sies Sulfur and selenium: the role of oxidation state in protein structure and function Angew. Chem., Int. Ed. Engl. 42 2003 4742 4758
3. S.J. Fairweather-Tait, and J. Dainty Use of stable isotopes to assess the bioavailability of trace elements: a review Food Addit. Contam. 19 2002 939 947
4. P. Van Dael, J. Lewis, and D. Barclay Stable isotope-enriched selenite and selenate tracers for human metabolic studies: a fast and accurate method for their preparation from elemental selenium and their identification and quantification using hydride generation atomic absorption spectrometry J. Trace Elem. Med. Biol. 18 2004 75 80
5. L. Zhong, E.S.J. Arnér, and A. Holmgren Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Proc. Natl. Acad. Sci. U. S. A. 97 2000 5854 5859
6. D.L. LeDuc, A.S. Tarun, M. Montes-Bayon, J. Meija, M.F. Malit, C.P. Wu, M. AbdelSamie, C.Y. Chiang, A. Tagmount, M. deSouza, B. Neuhierl, A. Böck, J. Caruso, and N. Terry Overexpression of selenocysteine methyltransferase in Arabidopsis and Indian mustard increases selenium tolerance and accumulation Plant Physiol. 135 2004 377 383
7. C.D. Thomson Assessment of requirements for selenium and adequacy of selenium status: a review Eur. J. Clin. Nutr. 58 2004 391 402
8. M.P. Rayman The importance of selenium to human health Lancet 356 2000 233 241
9. L.C. Clark, G.F. Combs Jr., B.W. Turnbull, E.H. Slate, D.K. Chalker, J. Chow, L.S. Davis, R.A. Glover, G.F. Graham, E.G. Gross, A. Krongrad, J.L. Lesher Jr., H.K. Park, B.B. Sanders Jr., C.L. Smith, and J.R. Taylor Effects of selenium supplementation for cancer prevention in patients with carcinoma of the skin. A randomized controlled trial. Nutritional Prevention of Cancer Study Group JAMA 276 1996 1957 1963
10. E.A. Klein Selenium and vitamin E cancer prevention trial Ann. N. Y. Acad. Sci. 1031 2004 234 241
11. M.R. Bösl, K. Takaku, M. Oshima, S. Nishimura, and M.M. Taketo Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp) Proc. Natl. Acad. Sci. U. S. A. 94 1997 5531 5534
12. G.V. Kryukov, S. Castellano, S.V. Novoselov, A.V. Lobanov, O. Zehtab, R. Guigo, and V.N. Gladyshev Characterization of mammalian selenoproteomes Science 300 2003 1439 1443
13. L. Flohe, W.A. Gunzler, and H.H. Schock Glutathione peroxidase: a selenoenzyme FEBS Lett. 32 1973 132 134
14. J.R. Arthur The glutathione peroxidases Cell. Mol. Life Sci. 57 2000 1825 1835
15. F. Ursini, M. Maiorino, R. Brigelius-Flohe, K.D. Aumann, A. Roveri, D. Schomburg, and L. Flohe Diversity of glutathione peroxidases Methods Enzymol. 252 1995 38 53
16. J. Köhrle The deiodinase family: selenoenzymes regulating thyroid hormone availability and action Cell. Mol. Life Sci. 57 2000 1853 1863
17. G. Mugesh, L.O. Klotz, W.W. du Mont, K. Becker, and H. Sies Selenenyl iodide: a new substrate for mammalian thioredoxin reductase Org. Biomol. Chem. 1 2003 2848 2852
18. M.J. Berry, J.D. Kieffer, J.W. Harney, and P.R. Larsen Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase J. Biol. Chem. 266 1991 14155 14158
19. C. Buettner, J.W. Harney, and P.R. Larsen The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase Endocrinology 141 2000 4606 4612
20. G.G. Kuiper, W. Klootwijk, and T.J. Visser Substitution of cysteine for selenocysteine in the catalytic center of type III iodothyronine deiodinase reduces catalytic efficiency and alters substrate preference Endocrinology 144 2003 2505 2513
21. D. Salvatore, J.W. Harney, and P.R. Larsen Mutation of the Secys residue 266 in human type 2 selenodeiodinase alters 75Se incorporation without affecting its biochemical properties Biochimie 81 1999 535 538
22. E.S.J. Arnér, and A. Holmgren Physiological functions of thioredoxin and thioredoxin reductase Eur. J. Biochem. 267 2000 6102 6109
23. S. Gromer, S. Urig, and K. Becker The thioredoxin system-From science to clinic Med. Res. Rev. 24 2004 40 89
24. M. Matsui, M. Oshima, H. Oshima, K. Takaku, T. Maruyama, J. Yodoi, and M.M. Taketo Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene Dev. Biol. 178 1996 179 185
25. L. Nonn, R.R. Williams, R.P. Erickson, and G. Powis The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice Mol. Cell. Biol. 23 2003 916 922
26. C. Jakupoglu, G.K. Przemeck, M. Schneider, S.G. Moreno, N. Mayr, A.K. Hatzopoulos, M.H. de Angelis, W. Wurst, G.W. Bornkamm, M. Brielmeier, and M. Conrad Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development Mol. Cell. Biol. 25 2005 1980 1988
27. M. Conrad, C. Jakupoglu, S.G. Moreno, S. Lippl, A. Banjac, M. Schneider, H. Beck, A.K. Hatzopoulos, U. Just, F. Sinowatz, W. Schmahl, K.R. Chien, W. Wurst, G.W. Bornkamm, and M. Brielmeier Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function Mol. Cell. Biol. 24 2004 9414 9423
28. L. Zhong, E.S.J. Arnér, J. Ljung, F. Åslund, and A. Holmgren Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue J. Biol. Chem. 273 1998 8581 8591
29. L. Zhong, and A. Holmgren Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations J. Biol. Chem. 275 2000 18121 18128
30. L.D. Arscott, S. Gromer, R.H. Schirmer, K. Becker, and C.H. Williams Jr. 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 Proc. Natl. Acad. Sci. U. S. A. 94 1997 3621 3626
31. S. Gromer, L.D. Arscott, C.H. Williams Jr., R.H. Schirmer, and K. Becker Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds J. Biol. Chem. 273 1998 20096 20101
32. T. Sandalova, L. Zhong, Y. Lindqvist, A. Holmgren, and G. Schneider Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme Proc. Natl. Acad. Sci. U. S. A. 98 2001 9533 9538
33. C. Buettner, J.W. Harney, and M.J. Berry The Caenorhabditis elegans homologue of thioredoxin reductase contains a selenocysteine insertion sequence (SECIS) element that differs from mammalian SECIS elements but directs selenocysteine incorporation J. Biol. Chem. 274 1999 21598 21602
34. V.N. Gladyshev, M. Krause, X.M. Xu, K.V. Korotkov, G.V. Kryukov, Q.A. Sun, B.J. Lee, J.C. Wootton, and D.L. Hatfield Selenocysteine-containing thioredoxin reductase in C. elegans Biochem. Biophys. Res. Commun. 259 1999 244 249
35. F. Missirlis, J.K. Ulschmid, M. Hirosawa-Takamori, S. Gronke, U. Schafer, K. Becker, J.P. Phillips, and H. Jackle Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability J. Biol. Chem. 277 2002 11521 11526
36. I.Y. Kim, M.J. Guimaraes, A. Zlotnik, J.F. Bazan, and T.C. Stadtman Fetal mouse selenophosphate synthetase 2 (SPS2): characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system Proc. Natl. Acad. Sci. U. S. A. 94 1997 418 421
37. G.V. Kryukov, R.A. Kumar, A. Koc, Z. Sun, and V.N. Gladyshev Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase Proc. Natl. Acad. Sci. U. S. A. 99 2002 4245 4250
38. S. Bar-Noy, and J. Moskovitz Mouse methionine sulfoxide reductase B: effect of selenocysteine incorporation on its activity and expression of the seleno-containing enzyme in bacterial and mammalian cells Biochem. Biophys. Res. Commun. 297 2002 956 961
39. J.C. Boyington, V.N. Gladyshev, S.V. Khangulov, T.C. Stadtman, and P.D. Sun Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster Science 275 1997 1305 1308
40. M.J. Axley, A. Böck, and T.C. Stadtman Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium Proc. Natl. Acad. Sci. U. S. A. 88 1991 8450 8454
41. V.N. Gladyshev, S.V. Khangulov, M.J. Axley, and T.C. Stadtman Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 91 1994 7708 7711
42. Y. Zhang, and V.N. Gladyshev An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genes Bioinformatics 2005 2580 2589
43. D.C. Turner, and T.C. Stadtman Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein Arch. Biochem. Biophys. 154 1973 366 381
44. J.R. Andreesen Glycine reductase mechanism Curr. Opin. Chem. Biol. 8 2004 454 461
45. G.E. Garcia, and T.C. Stadtman Selenoprotein A component of the glycine reductase complex from Clostridium purinolyticum: nucleotide sequence of the gene shows that selenocysteine is encoded by UGA J. Bacteriol. 173 1991 2093 2098
46. S. Kreimer, and J.R. Andreesen Glycine reductase of Clostridium litorale. Cloning, sequencing, and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation Eur. J. Biochem. 234 1995 192 199
47. R.A. Arkowitz, and R.H. Abeles Mechanism of action of clostridial glycine reductase: isolation and characterization of a covalent acetyl enzyme intermediate Biochemistry 30 1991 4090 4097
48. M. Wagner, D. Sonntag, R. Grimm, A. Pich, C. Eckerskorn, B. Söhling, and J.R. Andreesen Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis Eur. J. Biochem. 260 1999 38 49
49. A. Böck, K. Forchhammer, J. Heider, and C. Baron Selenoprotein synthesis: an expansion of the genetic code Trends Biochem. Sci. 16 1991 463 467
50. V.N. Gladyshev, and G.V. Kryukov Evolution of selenocysteine-containing proteins: significance of identification and functional characterization of selenoproteins BioFactors 14 2001 87 92
51. V.N. Gladyshev, G.V. Kryukov, D.E. Fomenko, and D.L. Hatfield Identification of trace element-containing proteins in genomic databases Annu. Rev. Nutr. 24 2004 579 596
52. G.V. Kryukov, and V.N. Gladyshev Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues Genes Cells 5 2000 1049 1060
53. C. Thisse, A. Degrave, G.V. Kryukov, V.N. Gladyshev, S. Obrecht-Pflumio, A. Krol, B. Thisse, and A. Lescure Spatial and temporal expression patterns of selenoprotein genes during embryogenesis in zebrafish Gene Expr. Patterns 3 2003 525 532
54. A.P. Shuber, E.C. Orr, M.A. Recny, P.F. Schendel, H.D. May, N.L. Schauer, and J.G. Ferry Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum J. Biol. Chem. 261 1986 12942 12947
55. G.V. Kryukov, and V.N. Gladyshev The prokaryotic selenoproteome EMBO Rep. 5 2004 538 543
56. T. Obata, and Y. Shiraiwa A novel eukaryotic selenoprotein in the haptophyte alga Emiliania huxleyi J. Biol. Chem. 2005 18462 18468
57. S.M. Kanzok, A. Fechner, H. Bauer, J.K. Ulschmid, H.M. Muller, J. Botella-Munoz, S. Schneuwly, R. Schirmer, and K. Becker Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster Science 291 2001 643 646
58. S. Gromer, L. Johansson, H. Bauer, L.D. Arscott, S. Rauch, D.P. Ballou, C.H. Williams Jr., R.H. Schirmer, and E.S.J. Arnér Active sites of thioredoxin reductases: why selenoproteins? Proc. Natl. Acad. Sci. U. S. A. 100 2003 12618 12623
59. Z.-P. Wu, and D. Hilvert Conversion of a protease into an acyl transferase: selenosubtilisin J. Am. Chem. Soc. 111 1989 4513
60. M.D. Gieselman, Y. Zhu, H. Zhou, D. Galonic, and W.A. van der Donk Selenocysteine derivatives for chemoselective ligations ChemBioChem 3 2002 709 716
61. R.J. Hondal, and R.T. Raines Semisynthesis of proteins containing selenocysteine Methods Enzymol. 347 2002 70 83
62. R. Quaderer, A. Sewing, and D. Hilvert Selenocysteine-mediated native chemical ligation Helv. Chim. Acta 84 2001 1197 1206
63. L. Moroder Isosteric replacement of sulfur with other chalcogens in peptides and proteins J. Pept. Sci. 11 2005 187 214
64. A. Böck, K. Forchhammer, J. Heider, W. Leinfelder, G. Sawers, B. Veprek, and F. Zinoni Selenocysteine: the 21st amino acid Mol. Microbiol. 5 1991 515 520
65. T.C. Stadtman Selenocysteine Annu. Rev. Biochem. 65 1996 83 100
66. G.M. Lacourciere, H. Mihara, T. Kurihara, N. Esaki, and T.C. Stadtman Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate J. Biol. Chem. 275 2000 23769 23773
67. G.M. Lacourciere, and T.C. Stadtman Utilization of selenocysteine as a source of selenium for selenophosphate biosynthesis BioFactors 14 2001 69 74
68. P.R. Copeland Regulation of gene expression by stop codon recoding: selenocysteine Gene 312 2003 17 25
69. S.C. Low, and M.J. Berry Knowing when not to stop: selenocysteine incorporation in eukaryotes Trends Biochem. Sci. 21 1996 203 208
70. A. Krol Evolutionarily different RNA motifs and RNA-protein complexes to achieve selenoprotein synthesis Biochimie 84 2002 765 774
71. M. Rother, A. Resch, R. Wilting, and A. Böck Selenoprotein synthesis in archaea BioFactors 14 2001 75 83
72. M. Rother, R. Wilting, S. Commans, and A. Böck Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii J. Mol. Biol. 299 2000 351 358
73. D. Fagegaltier, N. Hubert, K. Yamada, T. Mizutani, P. Carbon, and A. Krol Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation EMBO J. 19 2000 4796 4805
74. P.R. Copeland, J.E. Fletcher, B.A. Carlson, D.L. Hatfield, and D.M. Driscoll A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs EMBO J. 19 2000 306 314
75. M.J. Berry, G.W. Martin III, R. Tujebajeva, E. Grundner-Culemann, J.B. Mansell, N. Morozova, and J.W. Harney Selenocysteine insertion sequence element characterization and selenoprotein expression Methods Enzymol. 347 2002 17 24
76. A. Mehta, C.M. Rebsch, S.A. Kinzy, J.E. Fletcher, and P.R. Copeland Efficiency of mammalian selenocysteine incorporation J. Biol. Chem. 279 2004 37852 37859
77. S. Muller, H. Senn, B. Gsell, W. Vetter, C. Baron, and A. Böck The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: biosynthesis and characterization of (Se)2-thioredoxin Biochemistry 33 1994 3404 3412
78. G.T. Chen, M.J. Axley, J. Hacia, and M. Inouye Overproduction of a selenocysteine-containing polypeptide in Escherichia coli: the fdhF gene product Mol. Microbiol. 6 1992 781 785
79. J. Heider, and A. Böck Targeted insertion of selenocysteine into the alpha subunit of formate dehydrogenase from Methanobacterium formicicum J. Bacteriol. 174 1992 659 663
80. E.S.J. Arnér, H. Sarioglu, F. Lottspeich, A. Holmgren, and A. Böck 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 1999 1003 1016
81. O. Rengby, L. Johansson, L.A. Carlson, E. Serini, A. Vlamis-Gardikas, P. Kårsnäs, and E.S.J Arnér Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis Appl. Environ. Microbiol. 70 2004 5159 5167
82. P. Tormay, A. Sawers, and A. Böck Role of stoichiometry between mRNA, translation factor SelB and selenocysteyl-tRNA in selenoprotein synthesis Mol. Microbiol. 21 1996 1253 1259
83. J.B. Mansell, D. Guevremont, E.S. Poole, and W.P. Tate A dynamic competition between release factor 2 and the tRNA(Sec) decoding UGA at the recoding site of Escherichia coli formate dehydrogenase H EMBO J. 20 2001 7284 7293
84. L. Johansson, C. Chen, J. Thorell, A. Fredriksson, S. Stone-Elander, G. Gafvelin, and E.S.J. Arnér Exploiting the 21st amino acid-purifying and labeling proteins by selenolate targeting Nat. Methods 1 2004 61 66
85. E.S.J. Arnér Recombinant expression of mammalian selenocysteine-containing thioredoxin reductase and other selenoproteins in Escherichia coli Methods Enzymol. 347 2002 226 235
86. S. Hazebrouck, L. Camoin, Z. Faltin, A.D. Strosberg, and Y. Eshdat Substituting selenocysteine for catalytic cysteine 41 enhances enzymatic activity of plant phospholipid hydroperoxide glutathione peroxidase expressed in Escherichia coli J. Biol. Chem. 275 2000 28715 28721
87. Z. Jiang, E.S.J. Arnér, Y. Mu, L. Johansson, J. Shi, S. Zhao, S. Liu, R. Wang, T. Zhang, G. Yan, J. Liu, J. Shen, and G. Luo Expression of selenocysteine-containing glutathione S-transferase in Escherichia coli Biochem. Biophys. Res. Commun. 321 2004 94 101
88. S. Müller, J. Heider, and A. Böck The path of unspecific incorporation of selenium in Escherichia coli Arch. Microbiol. 168 1997 421 427
89. E.S.J. Arnér, H. Sarioglu, F. Lottspeich, A. Holmgren, and A. Böck 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 1999 1003 1016
90. M. Fassbender, D. de Villiers, M. Nortier, and N. van der Walt The natBr(p,x) (73,75)Se nuclear processes: a convenient route for the production of radioselenium tracers relevant to amino acid labelling Appl. Radiat. Isotopes 54 2001 905 913
91. R. Bergmann, P. Brust, G. Kampf, H.H. Coenen, and G. Stocklin Evaluation of radioselenium labeled selenomethionine, a potential tracer for brain protein synthesis by PET Nucl. Med. Biol. 22 1995 475 481
92. W.A. Hendrickson, J.R. Horton, and D.M. LeMaster Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure EMBO J. 9 1990 1665 1672
93. M.P. Strub, F. Hoh, J.F. Sanchez, J.M. Strub, A. Böck, A. Aumelas, and C. Dumas Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing Structure (Camb.) 11 2003 1359 1367
94. J.F. Sanchez, F. Hoh, M.P. Strub, A. Aumelas, and C. Dumas Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein Structure (Camb.) 10 2002 1363 1370
95. H. Duddeck Selenium-77 nuclear magnetic resonance spectroscopy Prog. Nucl. Magn. Reson. Spectrosc. 27 1995 1 323
96. J.O. Boles, W.H. Tolleson, J.C. Schmidt, R.B. Dunlap, and J.D. Odom Selenomethionyl dihydrofolate reductase from Escherichia coli. Comparative biochemistry and 77Se nuclear magnetic resonance spectroscopy J. Biol. Chem. 267 1992 22217 22223
97. P. Gettins, and B.C. Crews 77Se NMR characterization of 77Se-labeled ovine erythrocyte glutathione peroxidase J. Biol. Chem. 266 1991 4804 4809
98. E. Stocking, J. Schwarz, H. Senn, M. Salzmann, and L. Silks Synthesis of l-selenocysteine, l-[77Se]selenocysteine and l-tellurocystine J. Chem. Soc., Perkin. Trans. 1 1997 2443 2447
99. D. Besse, N. Budisa, W. Karnbrock, C. Minks, H.J. Musiol, S. Pegoraro, F. Siedler, E. Weyher, and L. Moroder Chalcogen-analogs of amino acids. Their use in X-ray crystallographic and folding studies of peptides and proteins Biol. Chem. 378 1997 211 218
100. S. Pegoraro, S. Fiori, S. Rudolph-Bohner, T.X. Watanabe, and L. Moroder Isomorphous replacement of cystine with selenocystine in endothelin: oxidative refolding, biological and conformational properties of [Sec3,Sec11,Nle7]- endothelin-1 J. Mol. Biol. 284 1998 779 792
101. I.M. Bell, M.L. Fisher, Z.P. Wu, and D. Hilvert Kinetic studies on the peroxidase activity of selenosubtilisin Biochemistry 32 1993 3754 3762
102. L. Ding, Z. Liu, Z. Zhu, G. Luo, D. Zhao, and J. Ni Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic Biochem. J. 332 Pt. 1 1998 251 255
103. G.M. Luo, Z.Q. Zhu, L. Ding, G. Gao, Q.A. Sun, Z. Liu, T.S. Yang, and J.C. Shen Generation of selenium-containing abzyme by using chemical mutation Biochem. Biophys. Res. Commun. 198 1994 1240 1247
104. S. Boschi-Muller, S. Muller, A. Van Dorsselaer, A. Böck, and G. Branlant Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity FEBS Lett. 439 1998 241 245
105. H.J. Yu, J.Q. Liu, A. Böck, J. Li, G.M. Luo, and J.C. Shen Engineering glutathione transferase to a novel glutathione peroxidase mimic with high catalytic efficiency: incorporation of selenocysteine into glutathione-binding scaffold using auxotrophic expression system J. Biol. Chem. 2005 11930 11935
106. S. Ma, R.M. Caprioli, K.E. Hill, and R.F. Burk Loss of selenium from selenoproteins: conversion of selenocysteine to dehydroalanine in vitro J. Am. Soc. Mass Spectrom. 14 2003 593 600
107. V.N. Gladyshev, K.-T. Jeang, and T.C. Stadtman Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene Proc. Natl. Acad. Sci. U. S. A. 93 1996 6146 6151
108. J. Nordberg, L. Zhong, A. Holmgren, and E.S.J. Arnér Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue J. Biol. Chem. 273 1998 10835 10842
109. R.D. Hoffman, and M.D. Lane Iodophenylarsine oxide and arsenical affinity chromatography: new probes for dithiol proteins. Application to tubulins and to components of the insulin receptor-glucose transporter signal transduction pathway J. Biol. Chem. 267 1992 14005 14011
110. E. Kalef, P.G. Walfish, and C. Gitler Arsenical-based affinity chromatography of vicinal dithiol-containing proteins: purification of L1210 leukemia cytoplasmic proteins and the recombinant rat c-erb A beta 1 T3 receptor Anal. Biochem. 212 1993 325 334
111. G.Y. Zhou, M. Jauhiainen, K. Stevenson, and P.J. Dolphin Human plasma lecithin:cholesterol acyltransferase. Preparation and use of immobilized p-aminophenylarsenoxide as a catalytic site-directed covalent ligand in enzyme purification J. Chromatogr. 568 1991 69 83
112. R.E. Huber, and R.S. Criddle Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs Arch. Biochem. Biophys. 122 1967 164 173
113. C. Rocher, J.L. Lalanne, and J. Chaudiere Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase Eur. J. Biochem. 205 1992 955 960
114. M. Maiorino, K.D. Aumann, R. Brigelius-Flohe, D. Doria, J. van den Heuvel, J. McCarthy, A. Roveri, F. Ursini, and L. Flohe Probing the presumed catalytic triad of a selenium-containing peroxidase by mutational analysis Z. Erzieh.Wiss. 37 Suppl. 1 1998 118 121
115. S. Bar-Noy, S.N. Gorlatov, and T.C. Stadtman Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity Free Radic. Biol. Med. 30 2001 51 61
116. S.R. Lee, S. Bar-Noy, J. Kwon, R.L. Levine, T.C. Stadtman, and S.G. Rhee 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 Proc. Natl. Acad. Sci. U. S. A. 97 2000 2521 2526
117. G.E. Garcia, and T.C. Stadtman Clostridium sticklandii glycine reductase selenoprotein A gene: cloning, sequencing, and expression in Escherichia coli J. Bacteriol. 174 1992 7080 7089
118. M.D. Gieselman, L. Xie, and W.A. van Der Donk Synthesis of a selenocysteine-containing peptide by native chemical ligation Org. Lett. 3 2001 1331 1334
119. N. Budisa, B. Steipe, P. Demange, C. Eckerskorn, J. Kellermann, and R. Huber High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli Eur. J. Biochem. 230 1995 788 796
120. S. Pegoraro, S. Fiori, J. Cramer, S. Rudolph-Bohner, and L. Moroder The disulfide-coupled folding pathway of apamin as derived from diselenide-quenched analogs and intermediates Protein Sci. 8 1999 1605 1613
121. L. Johansson, U. Svensson, G. Jacobsson-Ekman, E.S.J. Arnér, M. van Hage, A. Bucht, G. Gafvelin. A mouse model for in vivo tracking of the major dust mite allergen Der p 2 after inhalation, FEBS J. (in press).