From sulfur to selenium. A new research arena in chemical biology and biological chemistry

Current Chemical Biology

Volumn 7, Issue 1, 2013, Pages 2-24

  Iwaoka, Michio ^a   Arai, Kenta ^a  

^a TOKAI UNIVERSITY   (Japan)

Author keywords

Antioxidants; Protein folding; Selenocysteine; Selenoenzyme; Weak interaction

Indexed keywords

EBSELEN; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HOMOCYSTEINE; IODOTHYRONINE; ORGANOSELENIUM DERIVATIVE; RIBONUCLEASE A; SELENIDE; SELENIUM; SELENIUM DERIVATIVE; SELENOCYSTEINE; SELENOMETHIONINE; SELENOPROTEIN; SULFUR; THIOREDOXIN REDUCTASE;

AB INITIO CALCULATION; ACETYLATION; AMINO ACID SEQUENCE; ANTIOXIDANT ACTIVITY; APOPTOSIS; ASYMMETRIC SYNTHESIS; ATOM; BIOCHEMISTRY; BIOLOGICAL ACTIVITY; BIOSYNTHESIS; CATALYST; CHEMICAL MODIFICATION; CHEMICAL STRUCTURE; CONFORMATION; COVALENT BOND; DEIODINATION; DISSOCIATION; DISULFIDE BOND; ELECTRON; ENZYME ACTIVITY; HYDROGEN BOND; HYDROLYSIS; IONIZATION; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOPHILICITY; ORGANIC CHEMISTRY; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PEPTIDE SYNTHESIS; PHOSPHORYLATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; PULSE RADIOLYSIS; RACEMIZATION; REACTION TIME; REVIEW; RING OPENING; SOLID STATE;

EID: 84878649077     PISSN: 22127968     EISSN: 18723136     Source Type: Journal    
DOI: 10.2174/2212796811307010002     Document Type: Review

References (217)

1. Buk RF, Ed. Selenium in biology and human health. New York: Springer-Verlag 1994.
2. Hatfield DL, Ed. Selenium: its molecular biology and role in human health. Boston: Kluwer Academic Publisher 2001.
3. Irons R, Carlson BA, Hatfield DL, Davis CD. Both selenoproteins and low molecular weight selenocompounds reduce colon cancer risk in mice with genetically impaired selenoprotein expression. J Nutr 2006; 136: 1311-7.
4. Kryukov GV, Castellano S, Novoselov SV, et al. Characterization of mammalian selenoproteomes. Science 2003; 300(5624): 1439-43.
5. Gromer S, Eubel JK, Lee BL, Jacob J. Human selenoproteins at a glance. Cell Mol Life Sci 2005; 62: 2414-37.
6. Papp LV, Lu J, Holmgren A, Khanna KK. From selenium to selenoproteins: synthesis, identity, and their role in human health. Antioxid Redox Signal 2007; 9(7): 775-806.
7. Jackson-Rosario SE, Self WT. Targeting selenium metabolism and selenoproteins: novel avenues for drug discovery. Metallomics 2010; 2: 112-6.
8. Flohé L, Günzler WA, Schock HH. Glutathione peroxidase: A selenoenzyme. FEBS Lett 1973; 32: 132-4.
9. Savaskan NE, Ufer C, Kühn H, Borchert A. Molecular biology of glutathione peroxidase 4: from genomic structure to developmental expression and neural function. Biol Chem 2007; 388: 1007-17.
10. Conrad M, Schneider M, Seiler A, Bornkamm GW. Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals. Biol Chem 2007; 388: 1019-25.
11. Toppo S, Flohé L, Ursini F, Vanin S, Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim Biophys Acta Gen Subj 2009; 1790: 1486-500.
12. Forstrom JW, Zakowski JJ, Tappel, AL. Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine. Biochemistry 1978; 17: 2639-44.
13. Holmgren A, Lu J. Thioredoxin and thioredoxin reductase: Current research with special reference to human disease. Biochem Biophys Res Commun 2010; 396: 120-4.
14. Prast-Nielsen Stefanie, Huang HH, Williams DL. Thioredoxin glutathione reductase: its role in redox biology and potential as a target for drugs against neglected diseases. Biochim Biophys Acta Gen Subj 2011; 1810: 1262-71.
15. Maia AL, Goemann IM, Meyer ELS, Wajner SM. Deiodinases: the balance of thyroid hormone: type 1 iodothyronine deiodinase in human physiology and disease. J Endocrinol 2011; 209: 283-7.
16. Williams GR. Bassett JHD. Deiodinases: the balance of thyroid hormone: local control of thyroid hormone action: role of type 2 deiodinase. J Endocrinol 2011; 209(3): 261-72.
17. Dentice M, Ambrosio R, Salvatore D. Role of type 3 deiodinase in cancer. Expert Opin Ther Targets 2009; 13: 1363-73.
18. Böck A, Forchhammer K, Heider J, Baron C. Selenoprotein synthesis: an expansion of the genetic code. Trends Biochem Sci 1991; 16: 463-7.
19. Low SC, Berry MJ. Knowing when not to stop: selenocysteine incorporation in eukaryotes. Trends Biochem Sci 1996; 21: 203-8.
20. Böck A, Forchhammer K, Heider J, et al. Selenocysteine: the 21st amino acid. Mol Microbiol 1991; 5: 515-20.
21. Hendrickson WA, Horton JR, LeMaster DM. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of threedimensional structure. EMBO J 1990; 9: 1665-72.
22. Uson I, Sheldrick GM. Advances in direct methods for protein crystallography. Curr Opin Struct Biol 1999; 9: 643-8.
23. Pegoraro S, Fiori S, Rudolph-Böhner S, Watanabe TX, Moroder L. Isomorphous replacement of cystine with selenocystine in endothelin: oxidative refolding, biological and conformational properties of [Sec3, Sec11, Nle7]-endothelin-1. J Mol Biol 1998; 284: 779-92.
24. Wu ZP, Hilvert D. Conversion of a protease into an acyl transferase: selenolsubtilisin. J Am Chem Soc 1989; 111: 4513-4.
25. van Dorst SH, Peterson PJ. Selenium speciation in the soil solution and its relevance to plant uptake. J Sci Food Agric 1984; 35: 601-5.
26. Tamura T, Oikawa T, Ohtaka A, Fujii N, Esaki N, Soda K. Synthesis and characterization of the selenium analog of glutathione disulfide. Anal Biochem 1993; 208: 151-4.
27. Park YC, Kim JB, Heo Y, et al. Metabolism of subtoxic level of selenite by double-perfused small intestine in rats. Biol Trace Elem Res 2004; 98: 143-57.
28. Beld J, Woycechowsky KJ, Hilvert D. Selenoglutathione: efficient oxidative protein folding by a diselenide. Biochemistry 2007; 46: 5382-90.
29. Beld J, Woycechowsky KJ, Hilvert D. Selenoglutathione: efficient oxidative protein folding by a diselenide. [Erratum to document cited in CA147:047601] Biochemistry 2009; 48: 4662.
30. Yoshida S, Kumakura F, Komatsu I, et al. Antioxidative glutathione peroxidase activity of selenoglutathione. Angew Chem Int Ed 2011; 50: 2125-8.
31. Singh FV, Wirth T. Selenium compounds as ligands and catalysts. In: Wirth T, Ed. Organoselenium chemistry: synthesis and reactions. Weinheim: Wiley-VCH Verlag GmbH & Co KGaA 2012; 321-360.
32. Tang K, Jin X, Yan He, Xie X, Liu C, Gong Q. Synthesis, crystal structure and optical limiting property of a novel octanuclear silver cluster complex with an aryl selenolate ligand. J Chem Soc Dalton Trans 2001; 1374-7.
33. Takimiya K, Otsubo T. Selenium-containing π-conjugated compounds for electronic molecular materials. Phosphorus Sulfur Silicon Relat Elem 2005; 180: 873-81.
34. Kumbhare LB, Jain VK, Phadnis PP, Nethaji M. Palladium(II) and platinum(II) 2-(methoxycarbonyl)ethylselenolates: synthesis, spectroscopy, structures and their conversion into metal selenide. J Organomet Chem 2007; 692: 1546-56.
35. Ie Y, Hirose T, Yao A, et al. Synthesis of tripodal anchor units bearing selenium functional groups and their adsorption behaviour on gold. Phys Chem Chem Phys 2009; 11: 4949-51.
36. Iwaoka M, Tomoda S. Physical- and bio-organic chemistry of nonbonded selenium{dot operator}{dot operator}{dot operator}oxigen interaction. Phosphorus Sulfur Silicon Relat Elem 2005; 180: 755-66.
37. Mukherjee AJ, Zade SS, Singh HB, Sunoj RB, Organoselenium chemistry: role of intramolecular interactions. Chem Rev 2010; 110: 4357-416.
38. Iwaoka M, Kumakura F. Applications of water-soluble selenides and selenoxides to protein chemistry. Phosphorus Sulfur Silicon Relat Elem 2008; 183: 1009-17.
39. Kumakura F, Mishra B, Priyadarsini KI, Iwaoka M. A watersoluble cyclic selenide with enhanced glutathione peroxidase-like catalytic activities. Eur J Org Chem 2010; 440-5.
40. Iwaoka M, Tomoda S. trans-3,4-Dihydroxy-1-selenolane oxide: a new reagent for rapid and quantitative formation of disulfide bonds in polypeptides. Chem. Lett 2000; 1400-1.
41. Arai K, Dedachi K, Iwaoka M. Rapid and quantitative disulfide bond formation for a polypeptide chain using a cyclic selenoxide reagent in an aqueous medium. Chem Eur J 2011; 17: 481-5.
42. Paulmier C. Selenium reagents and intermediates in organic synthesis. Oxford: Pergamon Press 1986; 4-24.
43. Arnold AP, Tan KS, Rabenstein DL. Nuclear magnetic resonance studies of the solution chemistry of metal complexes. 23. Complexation of methylmercury by selenohydryl-containing amino acids and related molecules. Inorg Chem 1986; 25: 2433-7.
44. Tajc SG, Tolbert BS, Basavappa R, Miller BL. Direct determination of thiol pKa by isothermal titration microcalorimetry. J Am Chem Soc 2004; 126: 10508-9.
45. Silva VD, Woznichak MM, Burns KL, Grant KB, May SW. Selenium redox cycling in the protective effects of organoselenides against oxidant-induced DNA damage. J Am Chem Soc 2004; 126: 2409-13.
46. Kumar S, Singh HB, Wolmershäuser G. Protection against peroxynitrite- mediated nitration reaction by intramolecularly coordinated diorganoselenides. Organometallics 2006; 25(2): 382-93.
47. Seinmann D, Nauser T, Koppenol WH. Selenium and sulfur in exchange reaction: a comparative study. J Org Chem 2010; 75: 6696-9
48. Metanis N, Keinan E, Dawson PE. Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency. J Am Chem Soc 2006; 128: 16684-91.
49. Wood PM. The redox potential for dimethyl sulphoxide reduction to dimethyl sulphide. FEBS Lett 1980; 124: 11-4.
50. Rothwarf DM, Scheraga HA. Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution. Biochemistry 1993; 32: 2671-9.
51. Byun BJ, Kang YK. Conformational preferences and pKa value of selenocysteine residue. Biopolymers 2011; 95: 345-53.
52. Fujita K, Iwaoka M., Tomoda S. Synthesis of diaryl diselenides having chiral pyrrolidine rings with C2 symmetry. Their application to the asymmetric methoxyselenenylation of trans-β- methylstyrenes. Chem Lett 1994; 923-6.
53. Fujita K, Murata K, Iwaoka M, Tomoda S. Design of optically active selenium reagents having a chiral tertiary amino group and their application to asymmetric inter- and intramolecular oxyselenenylations. Tetrahedron 1997; 53: 2029-48.
54. Fragale G, Wirth T. Chiral diselenides in asymmetric cyclization reactions. Eur J Org Chem 1998; 1361-9.
55. Fragale G, Wirth T, Fragale G, Neuburger M. New and efficient selenium reagents for stereoselective selenenylation reactions. Chem Commun 1998; 1867-8.
56. Tiecco M, Testaferri L, Santi C, Tomassini C, Santoro S, Marini F, Bagnoli L, Temperini A, Costantino F. Intramolecular nonbonding interactions between selenium and sulfur - spectroscopic evidence and importance in asymmetric synthesis. Eur J Org Chem 2006; 4867-73.
57. Iwaoka M, Tomoda S. A model study on the effect of an amino group on the antioxidant activity of glutathione peroxidase. J Am Chem Soc 1994; 116: 2557-61.
58. Mugesh G, Panda A, Singh, HB, Punekar NS, Butcher RJ. Glutathione peroxidase-like antioxidant activity of diaryl diselenides: a mechanistic study. J Am Chem Soc 2001; 123: 839-50.
59. Back TG, Moussa Z. Remarkable activity of a novel cyclic seleninate ester as a glutathione peroxidase mimetic and its facile in situ generation from allyl 3-hydroxypropyl selenide. J Am Chem Soc 2002; 124: 12104-5.
60. Roy G, Nethaji M, Mugesh G. Biomimetic studies on anti-thyroid drugs and thyroid hormone synthesis. J Am Chem Soc 2004; 126: 2712-3.
61. Zade SS, Singh HB, Butcher RJ. The isolation and crystal structure of a cyclic selenenate ester derived from bis(2,6-diformyl-4-tertbutylphenyl) diselenide and its glutathione peroxidase-like activity. Angew Chem Int Ed 2044; 43: 4513-5.
62. Iwaoka M, Tomoda S. Direct observation of intramolecular interaction between a divalent selenium and a tertiary amine by means of single crystal X-ray analysis and NMR spectroscopy. Phosphorus Sulfur Silicon Relat Elem. 1992; 67: 125-30.
63. Iwaoka M, Tomoda S. Nature of the intramolecular Se...N nonbonded interaction of 2-selenobenzylamine derivatives. An experimental evaluation by 1H, 77Se, and 15N NMR spectroscopy. J Am Chem Soc 1996; 118: 8077-84.
64. Komatsu H, Iwaoka M, Tomoda S. Intramolecular nonbonded interaction between selenium and oxygen as revealed by 17O and 77Se NMR spectroscopy and natural bond orbital analysis. Chem Commun 1999; 205-6.
65. Iwaoka M, Komtasu H, Katsuda T, Tomoda S. Nature of nonbonded Se...O interactions characterized by 17O NMR spectroscopy and NBO and AIM analyses. J Am Chem Soc 2004; 126: 5309-17.
66. Iwaoka M, Komtasu H, Tomoda S. Characterization of an intramolecular nonbonded interaction between selenium and fluorine in solution. Chem Lett 1998; 969-70.
67. Iwaoka M, Komtasu H, Katsuda T, Tomoda S. Quantitative evaluation of weak nonbonded Se...F interactions and their remarkable nature as orbital interactions. J Am Chem Soc 2002; 124: 1902-9.
68. Iwaoka M, Katsuda T, Tomoda S, Harada J, Ogawa K. Heavy-row atom effects on the strength of the weak nonbonded interactions between divalent selenium and halogen atoms. Chem Lett 2002; 518-9.
69. Iwaoka M, Katsuda T, Komtasu H, Tomoda S. Experimental and theoretical studies on the nature of weak nonbonded interactions between divalent selenium and halogen atoms. J Org Chem 2005; 70: 321-7.
70. Harada T, Yoshida H, Ohno K, et al. Implications of intramolecular OH...Se hydrogen bonding and CH...O interaction in the conformational stabilization of 2-(methylseleno)ethanol studied by vibrational spectroscopy and density functional theory. J Phys Chem A 2001; 105(18): 4517-23.
71. Iwaoka M, Tomoda S. First observation of a C-H...Se "hydrogen bond". J Am Chem Soc 1994; 116: 4463-4.
72. Iwaoka M, Komatsu H, Tomoda S. Deuterium-induced isotope effects of a C-H...Se "hydrogen bond" on the IR and NMR spectra of 6H,12H-Dibenzo[b,f][1,5]diselenocin. Bull Chem Soc Jpn 1996; 69: 1825-8.
73. Carugo O. Stereochemistry of the interaction between methionine sulfur and the protein core. Biol Chem 1999; 380: 495-8.
74. Pal D, Chakrabarti P. Non-hydrogen bond interactions involving the methionine sulfur atom. J Biomol Struct Dyn 2001; 19: 115-28.
75. Iwaoka M, Takemoto S, Okada M, Tomoda S. Statistical characterization of nonbonded S...O interactions in proteins. Chem Lett 200; 132-133.
76. Iwaoka M, Takemoto S, Okada M, Tomoda S. Weak nonbonded SX (X = O, N, and S) interactions in proteins. Statistical and theoretical studies. Bull Chem Soc Jpn 2002; 75: 1611-25.
77. Iwaoka M, Takemoto S, Tomoda S. Statistical and theoretical investigations on the directionality of nonbonded S...O interactions. Implications for molecular design and protein engineering. J Am Chem Soc 2002; 124: 10613-20.
78. Kucsman A, Kapovits I. Nonbonded sulfur-oxygen interaction in organic sulfur compounds. In: Bernardi F, Csizmadia IG, Mangini A, Eds. Organic Sulfur Chemistry. Amsterdam: Elsevier 1985; 191-245.
79. Iwaoka M, Isozumi N. Possible roles of S...O and S...N interactions in the functions and evolution of phospholipase A2. BIOPHYSICS 2006; 2: 23-34.
80. Dennis EA. Diversity of group types, regulation, and function of phospholipase A2. J Biol Chem 1994; 269: 13057-60.
81. Jain MK, Gelb MH, Rogers J, Berg OG. Kinetic basis for interfacial catalysis by phospholipase A2. Methods Enzymol 1995; 249: 567-614.
82. Dijkstra BW, Drenth J, Kalk KH. Active site and catalytic mechanism of phospholipase A2. Nature 1981; 289: 604-6.
83. Sekar K, Yu BZ, Rogers J, et al. Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99. Biochemistry 1997; 36: 3104-14.
84. Ohno M, Chijiwa T, Oda-Ueda N, Ogawa T, Hattori S. Molecular evolution of myotoxic phospholipase A2 from snake venom. Toxicon 2003; 42: 841-54.
85. Yu BZ, Pan YH, Janssen MJW, Bahnson BJ, Jain MK. Kinetic and structural properties of disulfide engineered phospholipase A2: insight into the role of disulfide bonding patterns. Biochemistry 2005; 44: 3369-79.
86. Yuan J, Palioura S, Salazar JC, et al. RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc Natl Acad Sci USA 2006; 103: 18923-7.
87. Stock T. Selzer M. Rother M. In vivo requirement of selenophosphate for selenoprotein synthesis in archaea. Mol Microbiol 2010; 75: 149-60.
88. Itoh Y, Sekine S, Matsumoto E, et al. Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs. J Mol Biol 2009; 385(5): 1456-69.
89. Low SC, Grundner-Culemann E, Harney JW, Berry MJ. SECISSBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy. EMBO J 2000; 19: 6882-90.
90. Ouerdane L, Mester Z. Production and characterization of fully selenomethionine-labeled saccharomyces cerevisiae. J Agric Food Chem 2008; 56: 11792-9.
91. Leinfelder W, Zehelein E, Mandrand-Berthelot MA, Boeck A. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature 1988; 331: 723-5.
92. Makiyama A, Komatsu I, Iwaoka M, Yatagai M. One-pot conversion of serine and α-methylserine derivatives to the corresponding cysteines and selenocystines by using chalcogenophosphate reagents. Phosphorus Sulfur Silicon Relat Elem. 2011; 186: 125-33.
93. Moroder L. Isosteric replacement of sulfur with other chalcogens in peptides and proteins. J Pept Sci 2005; 11: 187-214.
94. Wessjohann LA, Schneider A, Abbas M, Brandt W. Selenium in chemistry and biochemistry in comparison to sulfur. Biol Chem 2007; 388: 997-1006.
95. Iwaoka M, Ooka R, Nakazato T, Yoshida S, Oishi S. Synthesis of selenocysteine and selenomethionine derivatives from sulfurcontaining amino acids. Chem Biodivers 2008; 5: 359-74.
96. Tanaka H, Soda K. Selenocysteine. Methods Enzymol 1987; 143: 240-3.
97. Chocat R, Esaki N, Tanaka H, Soda K. Synthesis of Lselenodjenkolate and its degradation with methionine γ-lyase. Anal Biochem 1985; 148: 485-9.
98. Phadnis PP, Mugesh G. Internally stabilized selenocysteine derivatives: syntheses, 77Se NMR and biomimetic studies. Org Biomol Chem 2005; 3: 2476-81.
99. Roy J, Gordon W, Schwartz IL, Walter R. Optically active selenium- containing amino acids. Synthesis of L-selenocystine and Lselenolanthionine. J Org Chem 1970; 35: 510-3.
100. Zhu Y, Gieselman MD, Zhou H, Averin O, van der Donk WA. Biomimetic studies on the mechanism of stereoselective lanthionine formation. Org Biomol Chem 2003; 1: 3304-15.
101. Cohen RJ, Fox DL, Salvatore RN. A novel and highly efficient synthetic route to unsymmetrical organoselenides using cesium bases. J Org Chem 2004; 69: 4265-8.
102. Metanis N, Keinan E, Dawson PE. Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency. J Am Chem Soc 2006; 128: 16684-91.
103. Sakai M, Hashimoto K, Shirahama H. Synthesis of optically pure β-phenylselenoalanine through serine-β-lactone: a useful precursor of dehydroalanine. Heterocycles 1997; 44: 319-24.
104. Okeley NM, Zhu Y, van der Donk WA. Facile chemoselective synthesis of dehydroalanine-containing peptides. Org Lett 2000; 2: 3603-6.
105. Braga AL, Vargas F, Sehnem JA, Braga RC. Efficient synthesis of chiral β-seleno amides via ring-opening reaction of 2-oxazolines and their application in the palladium-catalyzed asymmetric allylic alkylation. J Org Chem 2005; 70: 9021-4.
106. Braga AL, Schneider PH, Paixao MW, Deobald AM, Peppe C, Bottega DP. Chiral seleno-amines from indium selenolates. A straightforward synthesis of selenocysteine derivatives. J Org Chem 2006; 71: 4305-7.
107. Barton DHR, Bridon D, Herve Y, Potier P, Thierry J, Zard SZ. Synthesis of new tetraazamacrocycles by Pd-catalyzed amination of 1,8-dichloroanthracene and 1,8-dichloroanthra-9,10-quinone. Tetrahedron 1986; 42: 4983-6.
108. Reich HJ, Jasperse CP, Renga JM. Organoselenium chemistry. Alkylation of acid, ester, amide, and ketone enolates with bromomethyl benzyl selenide and sulfide. Preparation of selenocysteine derivatives. J Org Chem 1986; 51: 2981-8.
109. Iwaoka M, Haraki C, Ooka R, et al. Synthesis of selenocystine derivatives from cystine by applying the transformation reaction from disulfides to diselenides. Tetrahedron Lett 2006; 47: 3861-3.
110. Oae S, Togo H. Facile conversions of aliphatic sulfonic acids, sulfinic acids, thiols, sulfonates, thiolsulfonates, and disulfides to the corresponding alkyl iodides by triphenylphosphine/iodine. Synthesis 1981; 371-3.
111. Wood PT, Woollins JD. Phosphorus-selenium heterocycles. J Chem Soc Chem Commun 1988; 1190-1.
112. Gray IP, Bhattacharyya P, Slawin AMZ, Woollins JD. A new synthesis of (PhPSe2)2 (Woollins reagent) and its use in the synthesis of novel P-Se heterocycles. Chem Eur J 2005; 11: 6221-7.
113. Hua G, Woollins JD. Formation and reactivity of phosphorusselenium rings. Angew. Chem. Int. Ed. 2009; 48: 1368-77.
114. Pattenden G, Thom SM, Jones MF. Enantioselective synthesis of 2- alkyl substituted cysteines. Tetrahedron 1993; 49: 2131-8.
115. Bergeron RJ, Wiegand J, McManis JS, Bharti N. The design, synthesis, and evaluation of organ-specific iron chelators. J Med Chem 2006; 49: 7032-43.
116. Muttenthaler M, Alewood PF. Selenopeptide chemistry. J Pept Sci 2008; 14: 1223-39.
117. Novoselov SV, Rao M., Onoshko NV, et al. Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii. EMBO J 2002; 21: 3681-93.
118. Driscoll DM, Copeland PR. Mechanism and regulation of selenoprotein synthesis. Annu Rev Nutr 2003; 23: 17-40.
119. Zinoni F, Birkmann A, Stadtman TC, Boeck A. Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci USA 1986; 83: 4650-4.
120. Sandman KE, Benner JS, Noren CJ. Phage display of selenopeptides. J Am Chem Soc 2000; 122: 960-1.
121. Jiang Z, Arner ESJ, Mu Y, Johansson L, et al. Expression of selenocysteine- containing glutathione S-transferase in Escherichia coli. Biochem Biophys Res Commun 2004; 321: 94-101.
122. Rengby O, Johansson L, Carlson LA, et al. Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis. Appl Environ Microbiol 2004; 70: 5159-67.
123. Strub MP, Hoh F, Sanchez JF, et al. Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing. Structure 2003; 11: 1359-67.
124. Budisa N, Huber R, Golbik R, Minks C, Weyher E, Moroder L. Atomic mutations in annexin V. Thermodynamic studies of isomorphous protein variants. Eur J Biochem 1998; 253: 1-9.
125. Boschi-Muller S, Muller S, Dorsselaer AV, Böck A, Branlant G. Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity. FEBS Lett 1998; 439: 241-5.
126. Yu H, Liu J, Böck A, Li J, Luo G, Shen J. Engineering glutathione transferase to a novel glutathione peroxidase mimic with high catalytic efficiency: incorporation of selenocysteine into a glutathionebinding scaffold using an auxotrophic expression system. J Biol Chem 2005; 280: 11930-5.
127. Ge Y. Qi Z. Wang Y, et al. Engineered selenium-containing glutaredoxin displays strong glutathione peroxidase activity rivaling natural enzyme. Int. J. Biochem. Cell Biol 2009; 41: 900-6.
128. Wu ZP, Hilvert D. Selenosubtilisin as a glutathione peroxidase mimic. J Am Chem Soc 1990; 112: 5647-8.
129. Luo G, Zhu Z, Ding L, et al. Generation of selenium-containing abzyme by using chemical mutation. Biochem Biophys Res Commun 1994; 198: 1240-7.
130. Ren X, Jemth P, Board PG, et al. A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase. Chem Biol 2002; 9: 789-94.
131. Sun Y, Li T, Chen H, et al. Selenium-containing 15-Mer peptides with high glutathione peroxidase-like activity. J Biol Chem 2004; 279: 37235-40.
132. Liu J, Zhang K, Ren X, Luo G, Shen J. Bioimprinted protein exhibits glutathione peroxidase activity. Anal Chim Acta 2004; 504: 185-9.
133. Koide T, Itoh H, Otaka A, et al. Synthetic study on selenocystinecontaining peptides. Chem Pharm Bull 1993; 41: 502-66.
134. Besse D, Moroder L. Synthesis of selenocysteine peptides and their oxidation to diselenide-bridged compounds. J Pept Sci 1997; 3: 442-53.
135. Hondal RJ. Incorporation of selenocysteine into proteins using peptide ligation. Protein Pept Lett 2005; 12: 757-64.
136. Hondal RJ, Nilsson BL, Raines RT. Selenocysteine in native chemical ligation and expressed protein ligation. J Am Chem Soc 2001; 123: 5140-1.
137. Gieselman MD, Xie L, van der Donk WA. Synthesis of a selenocysteine- containing peptide by native chemical ligation. Org Lett 2001; 3: 1331-4.
138. Quaderer R, Sewing A, Hilvert D. Selenocysteine-mediated native chemical ligation. Helv Chim Acta 2001; 84: 1197-206.
139. Harris KM, Flemer S Jr, Hondal RJ. Studies on deprotection of cysteine and selenocysteine side-chain protecting groups. J Pept Sci 2007; 13: 81-93.
140. Moroder L, Besse D, Musiol HJ, Rudolph-Boehner S, Sideler F. Oxidative folding of cystine-rich peptides versus regioselective cysteine pairing strategies. Biopolymers 1996; 40: 207-34.
141. Oikawa T, Esaki N, Tanaka H, Soda K. Metalloselenonein, the selenium analog of metallothionein: synthesis and characterization of its complex with copper ions. Proc Natl Acad Sci USA 1991; 88: 3057-9.
142. Armishaw CJ, Daly NL, Nevin ST, Adams DJ, Craik DJ, Alewood PF. α-Selenoconotoxins, a new class of Potent α7 neuronal nicotinic receptor antagonists. J Bio Chem 2006; 281: 14136-43.
143. Rajarathnam K, Sykes BD, Dewald B, Baggiolini M, Clark-Lewis I. Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function. Biochemistry 1999; 38: 7653-8.
144. Besse D, Moroder L. Synthesis of selenocysteine peptides and their oxidation to diselenide-bridged compounds. J Pept Sci 1997; 3: 442-53.
145. Kent SBH. Total chemical synthesis of proteins. Chem Soc Rev 2009; 38: 338-51.
146. Quaderer R, Hilvert D. Selenocysteine-mediated backbone cyclization of unprotected peptides followed by alkylation, oxidative elimination or reduction of the selenol. Chem Commun 2002; 2620-1.
147. Gieselman MD, Zhu Y, Zhou H, Galonic D, van der Donk WA. Selenocysteine derivatives for chemoselective ligations. ChemBio- Chem 2002; 3: 709-16.
148. Hondal RJ, Raines RT. Semisynthesis of proteins containing selenocysteine. Methods Enzymol 2002; 347: 70-83.
149. McGrath NA, Raines RT. Chemoselectivity in chemical biology: acyl transfer reactions with sulfur and selenium. Accounts Chem Res 2011; 44: 752-61.
150. Roelfes G, Hilvert D. Incorporation of selenomethionine into proteins through selenohomocysteine-mediated ligation. Angew Chem Int Ed 2003; 42: 2275-7.
151. Ballihaut G, Pecheyran C, Mounicou S, et al. Multimode detection (LA-ICP-MS, MALDI-MS and nanoHPLC-ESI-MS2) in 1D and 2D gel electrophoresis for selenium-containing proteins. Trends Anal Chem 2007; 26: 183-90.
152. Ma S, Hill KE, Burk RF, Caprioli RM. Mass spectrometric determination of selenenylsulfide linkages in rat selenoprotein P. J Mass Spectrom 2005; 40: 400-4.
153. Ballihaut G, Tastet L, Pecheyran C, et al. Biosynthesis, purification and analysis of selenomethionyl calmodulin by gel electrophoresislaser ablation-ICP-MS and capillary HPLC-ICP-MS peptide mapping following in-gel tryptic digestion. J. Anal At Spectrom 2005; 20: 493-9.
154. Ruiz-Encinar J, Ouerdane L, Buchmann W, Tortajada J, Lobinski R, Szpunar J. Identification of water-soluble selenium-containing proteins in selenized yeast by size-exclusion-reversedphase HPLC/ICPMS followed by MALDI-TOF and electrospray Q-TOF mass spectrometry. Anal Chem 2003; 75: 3765-74.
155. Dernovics M, Giusti P, Lobinski R. ICP-MS-assisted nanoHPLCelectrospray Q/time-of-flight MS/MS selenopeptide mapping in Brazil nuts. J Anal At Spectrom 2007; 22: 41-50.
156. Zinn N, Winter D, Lehmann WD. Recombinant isotope labeled and selenium quantified proteins for absolute protein quantification. Anal Chem 2010; 82: 2334-40.
157. Ballihaut G, Kilpatrick LE, Davis WC. Detection, identification, and quantification of selenoproteins in a candidate human plasma standard reference material. Anal Chem 2011; 83: 8667-74.
158. Dernovics M, Far J, Lobinski R. Identification of anionic selenium species in Se-rich yeast by electrospray QTOF MS/MS and hybrid linear ion trap/orbitrap MSn. Metallomics 2009; 1: 317-29.
159. Capelo JL, Ximenez-Embun P, Madrid-Albarran Y, Camara C. Enzymatic probe sonication: enhancement of protease-catalyzed hydrolysis of selenium bound to proteins in yeast. Anal Chem 2004; 76: 233-7.
160. Far J, Preud'homme H, Lobinski R. Detection and identification of hydrophilic selenium compounds in selenium-rich yeast by size exclusion- microbore normal-phase HPLC with the on-line ICP-MS and electrospray Q-TOF-MS detection. Anal Chim Acta 2010; 657: 175-90.
161. Iwaoka M. Nucleophilic selenium. In: Wirth T, Ed. Organoselenium chemistry: synthesis and reactions. Weinheim: Wiley-VCH Verlag GmbH & Co KGaA 2012; 53-109.
162. Iwaoka M, Takahashi T, Tomoda S. Syntheses and structural characterization of water-soluble selenium reagents for the redox control of protein disulfide bonds. Heteroatom Chem 2001; 12: 293-9.
163. Maiorino M, Aumann KD, Brigelius-Flohé R, et al. Probing the presumed catalytic triad of selenium-containing peroxidases by mutational analysis of phospholipid hydroperoxide glutathione peroxidase (PHGPx). Biol Chem Hoppe-Seyler 1995; 376: 651-60.
164. Ursini F, Maiorino M, Roveri A. Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme? Biomed Environ Sci 1997; 10: 327-32.
165. Mugesh G, du Mont WW. Structure-activity correlation between natural glutathione peroxidase (GPx) and mimics: a biomimetic concept for the design and synthesis of more efficient GPx mimics. Chem Eur J 2001; 7: 1365-70.
166. Mugesh G, du Mont WW, Sies H. Chemistry of biologically important synthetic organoselenium compounds. Chem Rev 2001; 101: 2125-79.
167. Sarma BK, Mugesh G. Glutathione peroxidase (GPx)-like antioxidant activity of the organoselenium drug ebselen: unexpected complications with thiol exchange reactions. J Am Chem Soc 2005; 127: 11477-85.
168. Bhabak KP, Mugesh G. Amide-based glutathione peroxidase mimics: effect of secondary and tertiary amide substituents on antioxidant activity. Chem Asian J 2009; 4: 974-83.
169. Kunwar A, Mishra B, Barik A, Kumbhare LB, Pandey R, Jain VK, Priyadarsini KI. 3,3'-diselenodipropionic acid, an efficient peroxyl radical scavenger and a GPx mimic, protects erythrocytes (RBCs) from AAPH-induced hemolysis. Chem Res Toxicol 2007; 20: 1482-7.
170. Mishra B, Barik A, Kunwar A, Kumbhare LB, Priyadarsini KI, Jain VK. Correlating the GPx activity of selenocystine derivatives with one-electron redox reactions. Phosphorus Sulfur Silicon Relat Elem 2008; 183: 1018-25.
171. Kunwar A, Bansal P, Kumar SJ, et al. In vivo radioprotection studies of 3,3'-diselenodipropionic acid, a selenocystine derivative. Free Radical Biol Med 2010; 48(3), 399-410.
172. Yasuda K, Watanabe H, Yamazaki S, Toda S. Glutathione peroxidase activity of D,L-selenocystine and selenocystamine. Biochem Biophys Res Commun 1980; 96: 243-9.
173. Singh B, Bag PP, Kumakura F, Iwaoka M, Priyadarsini KI. Role of substrate reactivity in the glutathione peroxidase (GPx) activity of selenocystine. Bull Chem Soc Jpn 2010; 83: 703-8.
174. Bell IM, Fisher ML, Wu ZP, Hilvert D. Kinetic studies on the peroxidase activity of selenosubtilisin. Biochemistry 1993; 32: 3754-62.
175. Casi G, Hilvert D. Reinvestigation of a selenopeptide with purportedly high glutathione peroxidase activity. J Biol Chem 2007; 282: 30518-22.
176. Metanis N, Foletti C, Beld J, Hilvert D. Selenoglutathionemediated rescue of kinetically trapped intermediates in oxidative protein folding. Isr J Chem 2011; 51: 953-9.
177. Beld J, Woycechowsky KJ, Hilvert D. Catalysis of oxidative protein folding by small-molecule diselenides. Biochemistry 2008; 47: 6985-7.
178. Nishibayashi Y, Uemura S. Selenoxide elimination and [2,3]- sigmatropic rearrangement. In: Wirth T, Ed. Organoselenium chemistry: synthesis and reactions. Weinheim: Wiley-VCH Verlag GmbH & Co KGaA 2012; 287-320.
179. Krause RJ, Elfarra AA. Reduction of L-methionine selenoxide to seleno-L-methionine by endogenous thiols, ascorbic acid, or methimazole. Biochem Pharmacol 2009; 77, 134-40.
180. Xu MJ, Yang ZL, Liang ZZ, Zhou SN. Construction of a monascus purpureus mutant showing lower citrinin and higher pigment production by replacement of ctnA with pks1 without using vector and resistance gene. J Agric Food Chem 2009; 57: 9764-8.
181. Back TG, Moussa Z, Parvez M. The exceptional glutathione peroxidase- like activity of di(3-hydroxypropyl) selenide and the unexpected role of a novel spirodioxaselenanonane intermediate in the catalytic cycle. Angew Chem Int Ed 2004; 43: 1268-70.
182. De Silva V, Woznichak MM, Burns KL, Grant KB, May SW. Selenium redox cycling in the protective effects of organoselenides against oxidant-induced DNA damage. J Am Chem Soc 2004; 126: 2409-13.
183. Moroder H, Kreutz C, Lang K, Serganov A, Micura R. Synthesis, oxidation behavior, crystallization and structure of 2'-methylseleno guanosine containing RNAs. J Am Chem Soc 2006; 128: 9909-18.
184. Iwaoka M, Kumakura F, Yoneda M, et al. Direct observation of conformational folding coupled with disulphide rearrangement by using a water-soluble selenoxide reagent-a case of oxidative regeneration of ribonuclease A under weakly basic conditions. J Biochem 2008; 144: 121-30.
185. Arai K, Kumakura F, Iwaoka M. Characterization of kinetic and thermodynamic phases in the prefolding process of bovine pancreatic ribonuclease A coupled with fast SS formation and SS reshuffling. Biochemistry 2010; 49: 10535-42.
186. Singh BG, Thomas E, Kumakura F, Dedachi K, Iwaoka M, Priyadarsini KI. One-electron redox processes in a cyclic selenide and a selenoxide: a pulse radiolysis study. J Phys Chem A 2010; 114: 8271-7.
187. Madeja Z, Sroka J, Nystroem C, et al. The role of thioredoxin reductase activity in selenium-induced cytotoxicity. Biochem Pharmacol 2005; 69: 1765-72.
188. Lu J, Berndt C, Holmgren A. Metabolism of selenium compounds catalyzed by the mammalian selenoprotein thioredoxin reductase. Biochim Biophys Acta Gen Subj 2009; 1790: 1513-9.
189. Eckenroth BE, Rould MA, Hondal RJ, Everse SJ. Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and drosophila melanogaster thioredoxin reductases. Biochemistry 2007; 46: 4694-705.
190. Anestal K, Arner ESJ. Rapid induction of cell death by seleniumcompromised thioredoxin reductase 1 but not by the fully active enzyme containing selenocysteine. J Biol Chem 2003; 278: 15966-72.
191. Brandt W, Wessjohann LA. The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state. ChemBioChem 2005; 6: 386-94.
192. Vasil'ev AA, Engman L. Iodothyronine deiodinase mimics. Deiodination of o,o'-diiodophenols by selenium and tellurium reagents. J Org Chem 1998; 63: 3911-7.
193. Goto K, Sonoda D, Shimada K, Sase S, Kawashima T. Modeling of the 5′-deiodination of thyroxine by iodothyronine deiodinase: chemical corroboration of a selenenyl iodide intermediate. Angew Chem Int Ed 2010; 49: 545-7.
194. Manna D, Mugesh G. A chemical model for the inner-ring deiodination of thyroxine by iodothyronine deiodinase. Angew Chem Int Ed 2010; 49: 9246-9.
195. Manna D, Mugesh G. Deiodination of thyroid hormones by iodothyronine deiodinase mimics: does an increase in the reactivity alter the regioselectivity? J Am Chem Soc 2011; 133: 9980-3.
196. Bayse CA, Rafferty ER. Is halogen bonding the basis for iodothyronine deiodinase activity? Inorg Chem 2010; 49: 5365-7.
197. Buettner C, Harney JW, Larsen PR. The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase. Endocrinology 2000; 141: 4606-12.
198. Hendrickson WA. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 1991; 254: 51-8.
199. Lemke CT, Smith GD, Howell PL. S-SAD, Se-SAD and S/Se- SIRAS using Cu Kalpha radiation: why wait for synchrotron time?. Acta Crystallogr Sect D 2002; 58(Pt 12): 2096-101.
200. Moroder L, Musiol HJ, Götz M, Renner C. Synthesis of single- and multiple-stranded cystine-rich peptides. Biopolymers 2005; 80: 85-97.
201. Pegoraro S, Fiori S, Cramer J, Rudolph-Böhner S, Moroder L. The disulfide-coupled folding pathway of apamin as derived from diselenide- quenched analogs and intermediates. Protein Sci 1999; 8: 1605-13.
202. Fiori S, Pegoraro S, Rudolph-Bchner S, Cramer J, Moroder L. Synthesis and conformational analysis of apamin analogs with natural and non-natural cystine/selenocystine connectivities. Biopolymers 2000; 53: 550-64.
203. Walewska A, Zhang MM, Skalicky JJ., Yoshikami D, Olivera BM, Bulaj G. Integrated oxidative folding of cysteine/selenocysteine containing peptides: improving chemical synthesis of conotoxins. Angew Chem Int Ed 2009; 49: 2221-4.
204. Han TS, Zhang MM, Gowd KH, et al. Disulfide-depleted selenoconopeptides: simplified oxidative folding of cysteine-rich peptides. ACS Med Chem Lett 2010; 1: 140-4.
205. Gowd KH, Yarotskyy V, Elmslie KS, Skalicky JJ, Olivera BM, Bulaj G. Site-specific effects of diselenide bridges on the oxidative folding of a cystine knot peptide, ω-selenoconotoxin GVIA. Biochemistry 2010; 49: 2741-52.
206. Muttenthaler M, Nevin ST, Grishin AA, et al. Solving the α- conotoxin folding problem: efficient selenium-directed on-resin generation of more potent and stable nicotinic acetylcholine receptor antagonists. J Am Chem Soc 2010; 132: 3514-22.
207. Walewska A, Jaskiewicz A, Bulaj G, Rolka K. Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities. Chem Biol Drug Des 2010; 77: 93-7.
208. Narayan M, Welker E, Wedemeyer WJ, Scheraga HA. Oxidative folding of proteins. Acc Chem Res 2000; 33: 805-12.
209. Welker E, Wedemeyer WJ, Narayan M, Scheraga HA. Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins. Biochemistry 2001; 40: 9059-64.
210. Lees WJ. Small-molecule catalysts of oxidative protein folding. Curr Opin Chem Biol 2008; 12: 740-5.
211. Rothwarf DM, Scheraga HA. Regeneration of bovine pancreatic ribonuclease A. 3. Dependence on the nature of the redox reagent. Biochemistry 1993; 32: 2690-7.
212. Beld J, Woycechowsky KJ, Hilvert D. Diselenides as universal oxidative folding catalysts of diverse proteins. J Biotechnol 2010; 150: 481-9.
213. Beld J, Woycechowsky KJ, Hilvert D. Small-molecule diselenides catalyze oxidative protein folding in vivo. ACS Chem Biol 2010; 5: 177-82.
214. Cowan EA, Oldham CD, May SW. Identification of a thioselenurane intermediate in the reaction between phenylaminoalkyl selenoxides and glutathione. 2011; 506: 201-7.
215. Rothwarf DM, Li YJ, Scheraga HA. Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike threedisulfide intermediates involved in separate pathways. Biochemistry 1998; 37: 3760-6.
216. Welker E, Narayan M, Wedemeyer WJ, Scheraga HA. Structural determinants of oxidative folding in proteins. Proc Natl Acad Sci USA 2001; 98: 2312-6.
217. Bhuyan BJ, Mugesh G. Biological and biochemical aspects of selenium compounds. In: Wirth T, Ed. Organoselenium chemistry: synthesis and reactions. Weinheim: Wiley-VCH Verlag GmbH & Co KGaA 2012; 361-396.