Why Nature Chose Selenium

ACS Chemical Biology

Volumn 11, Issue 4, 2016, Pages 821-841

  Reich, Hans J ^b   Hondal, Robert J ^a  

^a UNIVERSITY OF VERMONT   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOCOPHEROL; CHALCOGEN; ENZYME; GLUTATHIONE PEROXIDASE; IODOTHYRONINE DEIODINASE; NUCLEOPHILE; REACTIVE OXYGEN METABOLITE; SELENIUM; SELENIUM OXIDE; SELENOCYSTEINE; SULFUR; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

ACIDITY; BIOGEOCHEMISTRY; BIOLOGY; CANCER PREVENTION; CARCINOGENESIS; CHEMICAL BOND; DIET SUPPLEMENTATION; DIETARY INTAKE; ELECTRON TRANSPORT; ELECTROPHILICITY; HUMAN; NEOPLASM; NONHUMAN; NUCLEOPHILICITY; OXIDATION REDUCTION REACTION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; REVIEW; COMPLICATION; DEFICIENCY; NATURAL SCIENCE; NUTRITIONAL DEFICIENCY;

DEFICIENCY DISEASES; HUMANS; NATURE; NEOPLASMS; SELENIUM;

EID: 84966264067     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00031     Document Type: Review

References (279)

1. Westheimer, F. H. (1987) Why Nature chose phosphates Science 235, 1173-1178 10.1126/science.2434996
2. Odom, J. D. (1983) Selenium biochemistry chemical and physical studies Struct. Bonding (Berlin) 54, 1-26 10.1007/BFb0111317
3. Stadtman, T. C. (1990) Selenocysteine Annu. Rev. Biochem. 59, 111-127 10.1146/annurev.bi.59.070190.000551
4. Stadtman, T. C. (1996) Selenocysteine Annu. Rev. Biochem. 65, 83-100 10.1146/annurev.bi.65.070196.000503
5. Flohé, L., Andreesen, J. R., Brigelius-Flohé, R., Maiorino, M., and Ursini, F. (2000) Selenium, the element of the moon, in life on Earth IUBMB Life 49, 411-420 10.1080/152165400410263
6. Köhrle, J., Brigelius-Flohé, R., Böck, A., Gärtner, R., Meyer, O., and Flohé, L. (2000) Selenium in biology: facts and medical perspectives Biol. Chem. 81, 849-864 10.1515/BC.2000.107
7. Birringer, M., Pilawa, P., and Flohé, F. (2002) Trends in selenium biochemistry Nat. Prod. Rep. 19, 693-718 10.1039/B205802M
8. Jacob, C., Giles, G. I., Giles, N. M., and Sies, H. (2003) Sulfur and selenium: the role of oxidation state in protein structure and function Angew. Chem., Int. Ed. 42, 4742-4758 10.1002/anie.200300573
9. Brandt, W. and Wessjohann, L. A. (2005) 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 6, 1-9 10.1002/cbic.200400276
10. Wessjohann, L. A., Schneider, A., Abbas, M., and Brandt, W. (2007) Selenium in chemistry and biochemistry in comparison to sulfur Biol. Chem. 388, 997-1006 10.1515/BC.2007.138
11. Arnér, E. S. (2010) Selenoproteins: What unique properties can arise with selenocysteine in place of cysteine? Exp. Cell Res. 316, 1296-1303 10.1016/j.yexcr.2010.02.032
12. Hondal, R. J. and Ruggles, E. L. (2011) Differing views of the role of selenium in thioredoxin reductase Amino Acids 41, 73-89 10.1007/s00726-010-0494-6
13. Metanis, N., Beld, J., and Hilvert, D. (2001) The chemistry of selenocysteine. In Patai's Chemistry of Functional Groups, John Wiley & Sons, Hoboken, NJ, pp 1-73.
14. Kasaikina, M. V., Hatfield, D. L., and Gladyshev, V. N. (2012) Understanding selenoprotein function and regulation through the use of rodent models Biochim. Biophys. Acta, Mol. Cell Res. 1823, 1633-1642 10.1016/j.bbamcr.2012.02.018
15. Nauser, T., Steinmann, D., and Koppenol, W. H. (2012) Why do proteins use selenocysteine instead of cysteine? Amino Acids 42, 39-44 10.1007/s00726-010-0602-7
16. Hondal, R. J., Marino, S. M., and Gladyshev, V. N. (2013) Selenocysteine in thiol/disulfide-like exchange reactions Antioxid. Redox Signaling 18, 1675-1689 10.1089/ars.2012.5013
17. Oldfield, J. E. (1974) The selenium story: some reflections on the "moon-metal N. Z. Vet. J. 22, 85-94 10.1080/00480169.1974.34140
18. Oldfield, J. E. (1995) SeRENDIPITY Chemtech 25 (3) 52-55
19. Trofast, J. (2011) Berzelius' Discovery of Selenium Chemistry International 33, 16-19
20. Pizzi, R. A. (2004) Jons Jacob Berzelius Today's Chemist at Work 54-57
21. Franke, K. W. (1934) A new toxicant occurring naturally in certain samples of plant foodstuffs I: Results obtained in preliminary feeding trials J. Nutr. 8, 597-608
22. Franke, K. W. (1934) A new toxicant occurring naturally in certain samples of plant foodstuffs II: The occurrence of the toxicant in the protein fraction J. Nutr. 8, 609-613
23. Robinson, W. O. (1933) Determination of selenium in wheat and soils J. Assoc. Off. Agric. Chem. 16, 423-432
24. Beath, D. A., Eppson, H. F., and Gilbert, C. S. (1935) Selenium and other toxic minerals in soils and vegetation Wyoming Agric. Exp. Sta. Bull. 206, 55-73
25. Franke, K. W. and Painter, E. P. (1936) Selenium in proteins from toxic foodstuffs I: Remarks on the occurrence and nature of the selenium present in a number of foodstuffs or their derived products Cereal Chem. 13, 67-70
26. Painter, E. P. and Franke, K. W. (1935) Selenium in proteins from toxic foodstuffs III: The removal of selenium from toxic protein hydrolysates J. Biol. Chem. 111, 643-651
27. Böck, A., Forchhammer, K., Heider, J., Leinfelder, W., Sawers, G., Veprek, B., and Zinoni, F. (1991) Selenocysteine: the 21st amino acid Mol. Microbiol. 5, 515-520 10.1111/j.1365-2958.1991.tb00722.x
28. Atkins, J. F. and Gesteland, R. F. (2000) The twenty-first amino acid Nature 407, 463-464 10.1038/35035189
29. Cone, J. E., Del Río, R. M., Davis, J. N., and Stadtman, T. C. (1976) Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety Proc. Natl. Acad. Sci. U. S. A. 73, 2659-2663 10.1073/pnas.73.8.2659
30. O'Toole, D., Raisbeck, M., Case, J. C., and Whitson, T. D. (1996) Selenium-induced ";blind staggers"; and related myths. A commentary on the extent of historical livestock losses attributed to selenosis on western US rangelands Vet. Pathol. 33, 109-116 10.1177/030098589603300117
31. Oldfield, J. E. (1987) The two faces of selenium J. Nutr. 117, 2002-2008
32. Pinsent, J. (1954) The need for selenite and molybdate in the formation of formate dehydrogenases by members of the Coliaerogenes group of bacteria Biochem. J. 57, 10-16 10.1042/bj0570010
33. Patterson, E. L., Milstrey, R., and Stokstad, E. L. R. (1957) Effect of selenium in preventing exudative diathesis in chicks Exp. Biol. Med. 95, 617-620 10.3181/00379727-95-23307
34. Schwarz, K., Bieri, J. G., Briggs, G. M., and Scott, M. L. (1957) Prevention of exudative diathesis in chicks by factor 3 and selenium Exp. Biol. Med. 95, 621-625 10.3181/00379727-95-23308
35. Schwarz, K. and Foltz, C. M. (1957) Selenium as an integral part of factor 3 against dietary liver degeneration J. Am. Chem. Soc. 79, 3292-3293 10.1021/ja01569a087
36. Schwarz, K. (1951) A protective factor in yeast against liver necrosis in rats Exp. Biol. Med. 78, 852-854 10.3181/00379727-78-19240
37. McCoy, K. E. M. and Weswig, P. H. (1969) Some selenium responses in the rat not related to vitamin E J. Nutr. 98, 383-389
38. Jukes, T. H. (1992) Antioxidants, nutrition, and evolution Prev. Med. 21, 270-276 10.1016/0091-7435(92)90025-D
39. Levander, O. A. (1991) Scientific rationale for the 1989 recommended dietary allowance for selenium J. Am. Diet. Assoc. 91, 1572-1576
40. http://www.who.int/water-sanitation-health/dwq/chemicals/seleniumsum.pdf (see page 433).
41. Jukes, T. H. (1983) Selenium, an "essential poison J. Appl. Biochem. 5, 233-234
42. Shamberger, R. J. (1983) Selenium and health. In Trace elements in health: A review of current issues (Rose, J., Ed.) pp 167-181, Elsevier, London.
43. Tan, J. A., Hou, S. F., Zhu, W. Y., Li, R. B., Zheng, D. X., Wang, M. Y., and (The Group of Environment and Endemic Disease). (1979) The Keshan disease in China: a study of the geographical epidemiology Acta Geographica Sinica 34, 85-104
44. Chen, J. (2012) An original discovery: selenium deficiency and Keshan disease (an endemic heart disease) Asia Pac. J. Clin. Nutr. 21, 320-326
45. Keshan Disease Research Group of the Chinese Academy of Medical Sciences. (1979) Observations on effect of sodium selenite in prevention of Keshan disease Chin. Med. J. 92, 471-476
46. Keshan Disease Research Group of the Chinese Academy of Medical Sciences. (1979) Epidemiologic studies on the etiologic relationship of selenium and Keshan disease Chin. Med. J. 92, 477-482
47. Sokoloff, L. (1988) Kashin-Beck Disease: Current status Nutr. Rev. 46, 113-119 10.1111/j.1753-4887.1988.tb05395.x
48. Gauntt, C. and Tracy, S. (1995) Deficient diet evokes nasty heart virus Nat. Med. 1, 405-406 10.1038/nm0595-405
49. Beck, M. A., Shi, Q., Morris, V. C., and Levander, O. A. (1995) Rapid genomic evolution of a non-virulent coxsackievirus B3 in selenium-deficient mice results in selection of identical virulent isolates Nat. Med. 1, 433-436 10.1038/nm0595-433
50. Yao, Y., Pei, F., and Kang, P. (2011) Selenium, iodine, and the relation with Kashin-Beck disease Nutrition 27, 1095-1100 10.1016/j.nut.2011.03.002
51. Mertz, W. (1981) The essential trace elements Science 213, 1332-1338 10.1126/science.7022654
52. Rotruck, J. T., Pope, A. L., Ganther, H. E., Swanson, A. B., Hafeman, D. G. F., and Hoekstra, W. G. (1973) Selenium: biochemical role as a component of glutathione peroxidase Science 179, 588-590 10.1126/science.179.4073.588
53. Flohé, L., Günzler, W. A., and Schock, H. H. (1973) Glutathione peroxidase. A selenoenzyme FEBS Lett. 32, 132-134 10.1016/0014-5793(73)80755-0
54. Thompson, J. N. and Scott, M. L. (1970) Impaired lipid and vitamin E absorption related to atrophy of the pancreas in selenium-deficient chicks J. Nutr. 100, 797-809
55. Weichselbaum, T. E. (1935) Cystine deficiency in the albino rat Q. J. Exp. Physiol. 25, 363-367 10.1113/expphysiol.1935.sp000693
56. Schwarz, K. (1965) The role of vitamin E, selenium, and related factors in experimental nutritional liver disease Fed. Proc. 24, 58-67
57. Trapp, A. L., Keahey, K. K., Whittenack, D. L., and Whitehair, C. K. (1970) Vitamin E-selenium deficiency in swine: differential diagnosis and nature of the field problem J. Am. Vet. Med. Assoc. 157, 289-300
58. Hoekstra, W. G. (1975) Biochemical function of selenium and its relation to vitamin E Fed. Proc. 34, 2083-2089
59. Levander, O. A. (1992) Selenium and sulfur in antioxidant protective systems: relationships with vitamin E and malaria Exp. Biol. Med. 200, 255-259 10.3181/00379727-200-43430
60. Combs, G. F., Jr., Noguchi, T., and Scott, M. L. (1975) Mechanisms of action of selenium and vitamin E in protection of biological membranes Fed. Proc. 34, 2090-2095
61. Whanger, P. D., Weswig, P. H., Oldfield, J. E., Cheeke, P. R., and Schmitz, J. A. (1976) Selenium and white muscle disease in lambs: effects of vitamin E and ethoxyquin Nutr. Rep. Int. 13, 159-173
62. Scott, M. L. (1970) Nutritional and metabolic interrelationships involving vitamin E, selenium, and cystine in the chicken Int. Z. Vitamin Forsch. 40, 334-343
63. Molnar, G. I. Investigation of the Biochemical and Nutritional Interrelationships Between Vitamin E and Selenium in the Albino Rat, Masters thesis, Vanderbilt University, 1965.
64. Muth, O. H., Oldfield, J. E., Remmert, L. F., and Schubert, J. R. (1958) Effects of selenium and vitamin E on white muscle disease Science 128, 1090-1091 10.1126/science.128.3331.1090
65. Tappel, A. L. (1980) Vitamin E and selenium protection from in vivo lipid peroxidation Ann. N. Y. Acad. Sci. 355, 18-31 10.1111/j.1749-6632.1980.tb21324.x
66. Hill, K. E., Motley, A. K., Li, X., May, J. M., and Burk, R. F. (2001) Combined selenium and vitamin E deficiency causes fatal myopathy in guinea pigs J. Nutr. 131, 1798-802
67. Maiorino, M., Coassin, M., Roveri, A., and Ursini, F. (1989) Microsomal lipid peroxidation: effect of vitamin E and its functional interaction with phospholipid hydroperoxide glutathione peroxidase Lipids 24, 721-726 10.1007/BF02535211
68. May, J. M., Morrow, J. D., and Burk, R. F. (2002) Thioredoxin reductase reduces lipid hydroperoxides and spares alpha-tocopherol Biochem. Biophys. Res. Commun. 292, 45-49 10.1006/bbrc.2002.6617
69. May, J. M., Mendiratta, S., Hill, K. E., and Burk, R. F. (1997) Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase J. Biol. Chem. 272, 22607-22610 10.1074/jbc.272.36.22607
70. Beck, M. A. (1997) Increased virulence of coxsackievirus B3 in mice due to vitamin E or selenium deficiency J. Nutr. 127, 966S-970S
71. Loscalzo, J. (2014) Keshan Disease, selenium deficiency, and the selenoproteome N. Engl. J. Med. 370, 1756-1760 10.1056/NEJMcibr1402199
72. Nelson, A. A., Fitzhugh, O. G., and Calvery, H. O. (1943) Liver tumors following cirrhosis caused by selenium in rat Cancer Res. 3, 230-236
73. Clayton, C. C. and Bauman, C. A. (1949) Diet and azo dye tumors: effect of diet during a period when the dye is not fed Cancer Res. 9, 575-582
74. Shamberger, R. J. and Rudolph, G. (1966) Protection against cocarcinogenesis by antioxidants Experientia 22, 116 10.1007/BF01900187
75. Harr, J. R., Bone, J. F., Tinsley, I. J., Weswig, P. H., and Yamamoto, R. S. (1966) Selenium toxicity in rats. II. Histopathology. In Selenium in Biomedicine (Muth, O. H., Oldfield, J. E., and Weswig, P. H., Eds.) pp 153-178, Proc. 1st Int. Symp., Oregon State University, 1967, AVI Publishing Co., Westport, CT.
76. Tinsley, I. J., Harr, J. R., Bone, J. F., Weswig, P. H., and Yamamoto, R. S. (1966) Selenium toxicity in rats. I. Growth and longevity. In Selenium in Biomedicine (Muth, O. H., Oldfield, J. E., and Weswig, P. H., Eds.) pp 141-152, Proc. 1st Int. Symp., Oregon State University, 1967, AVI Publishing Co., Westport, CT.
77. Harr, J. R., Exon, J. H., Weswig, P. H., and Whanger, P. D. (1973) Relationship of dietary selenium concentration, chemical cancer induction and tissue concentration of selenium in rats Clin. Toxicol. 6, 487-495 10.3109/15563657308990545
78. Frost, D. V. (1972) The two faces of selenium-can selenophobia be cured? In Critical Reviews in Toxicology (Hemphill, D., Ed.) pp 467-514, CRC Press, Boca Raton, FL.
79. Shamberger, R. J. and Frost, D. V. (1969) Possible protective effect of selenium against human cancer Can. Med. Assn. J. 104, 82-84
80. Kubota, J., Allaway, W. H., Carter, D. L., Gary, E. E., and Lazar, V. A. (1967) Selenium in crops in the United States in relation to selenium-responsive diseases of animals J. Agric. Food Chem. 15, 448-453 10.1021/jf60151a006
81. Allaway, W. H., Kubota, J., Losee, F., and Roth, M. (1968) Selenium, molybdenum, and vanadium in human blood Arch. Environ. Health 16, 342-348 10.1080/00039896.1968.10665069
82. Schrauzer, G. N., White, D. A., and Schnieder, C. J. (1977) Cancer mortality correlation studies III: Statistical association with dietary selenium intakes Bioinorg. Chem. 7, 23-31 10.1016/S0006-3061(00)80126-X
83. Koivistoinen, P. and Huttunen, J. K. (1986) Selenium in food and nutrition in Finland: An overview on research and action Ann. Clin. Res. 18, 13-17
84. Ip, C. and Ip, M. M. (1981) Chemoprevention of mammary tumorigenesis by a combined regimen of selenium and vitamin A Carcinogenesis 2, 915-918 10.1093/carcin/2.9.915
85. Clark, L. C. (1985) The epidemiology of selenium and cancer Federation Proc. 44, 2584-2589
86. Clark, L. C. and Combs, G. F., Jr. (1986) Selenium compounds and the prevention of cancer: Research needs and public health implications J. Nutr. 116, 170-173
87. Combs, G. F., Jr. and Clark, L. C. (1985) Can dietary selenium modify cancer risk? Nutr. Rev. 43, 325-331 10.1111/j.1753-4887.1985.tb02392.x
88. Combs, G. F., Jr. and Combs, S. B. (1986) The role of selenium in nutrition, pp 413-461, Academic Press, New York.
89. Salonen, J. T., Alfthan, G., Huttunen, J. K., and Puska, P. (1984) Association between serum selenium and the risk of cancer Am. J. Epidemiol. 120, 342-349
90. Blot, W. J., Li, J. Y., Taylor, P. R., Guo, W., Dawsey, S., Wang, G.-Q., Yang, C. S., Zheng, S.-F., Gail, M., Li, G.-Y., Yu, Y., Liu, B.-Q., Tangrea, J., Sun, Y.-H., Liu, F., Fraumeni, J. F., Zhang, Y.-H., Jr., and Li, B. (1993) Nutrition intervention trials in Linxian, China: supplementation with specific vitamin/mineral combinations, cancer incidence, and disease-specific mortality in the general population J. Natl. Cancer Inst. 85, 1483-1492 10.1093/jnci/85.18.1483
91. Ganther, H. E. and Lawrence, J. R. (1997) Chemical transformations of selenium in living organisms: Improved forms of selenium for cancer prevention Tetrahedron 53, 12299-12310 10.1016/S0040-4020(97)00561-9
92. Ip, C., Thompson, H. J., Zhu, Z., and Ganther, H. E. (2000) In vitro and in vivo studies of methylseleninic acid: evidence that a monomethylated selenium metabolite is critical for cancer chemoprevention Cancer Res. 60, 2882-2886
93. Felix, K., Gerstmeier, S., Kyriakopoulos, A., Howard, O. M., Dong, H. F., Eckhaus, M., Behne, D., Bornkamm, G. W., and Janz, S. (2004) Selenium deficiency abrogates inflammation-dependent plasma cell tumors in mice Cancer Res. 64, 2910-2917 10.1158/0008-5472.CAN-03-2672
94. Heinonen, O. P., Albanes, D., Virtamo, J., Taylor, P. R., Huttunen, J. K., Hartman, A. M., Haapakoski, J., Malila, N., Rautalahti, M., Ripatti, S., Maenpaa, H., Teerenhovi, L., Koss, L., Virolainen, M., and Edwards, B. K. (1998) Prostate cancer and supplementation with alpha-tocopherol and beta-carotene: incidence and mortality in a controlled trial J. Natl. Cancer Inst. 90, 440-446 10.1093/jnci/90.6.440
95. Willett, W. C. and Stampfer, M. J. (1988) Selenium and cancer Science 297, 573-574 10.1136/bmj.297.6648.573
96. Clark, L. C. and Alberts, D. S. (1995) Selenium and cancer: Risk or prevention? J. Natl. Cancer Inst. 87, 473-475 10.1093/jnci/87.7.473
97. Jackson, M. I. and Combs, G. F., Jr. (2008) Selenium and anticarcinogenesis: Underlying mechanisms Curr. Opin. Clin. Nutr. Metab. Care 11, 718-726 10.1097/MCO.0b013e3283139674
98. Ip, C. (1998) Lessons from basic research in selenium and cancer prevention J. Nutr. 128, 1845-1854
99. Schrauzer, G. N. (1976) Selenium and cancer: A review Bioinorg. Chem. 5, 275-281 10.1016/S0006-3061(00)82026-8
100. Clark, L. C., Combs, G. F., Jr., Turnbull, B. W., Slate, E. H., Chalker, D. K., Chow, J., Davis, L. S., Glover, R. A., Graham, G. F., Gross, E. G., Krongrad, A., Lesher, J. L., Jr., Park, H. K., Sanders, B. B., Jr., Smith, C. L., and Taylor, J. R. (1996) Effects of selenium supplementation for cancer prevention in patients with carcinoma of the skin. A randomized controlled trial JAMA 276, 1957-1963 10.1001/jama.1996.03540240035027
101. Lippman, S. M., Goodman, P. J., Klein, E. A., Parnes, H. L., Thompson, I. M., Jr., Kristal, A. R., Santella, R. M., Probstfield, J. L., Moinpour, C. M., Albanes, D., Taylor, P. R., Minasian, L. M., Hoque, A., Thomas, S. M., Crowley, J. J., Gaziano, J. M., Stanford, J. L., Cook, E. D., Fleshner, N. E., Lieber, M. M., Walther, P. J., Khuri, F. R., Karp, D. D., Schwartz, G. G., Ford, L. G., and Coltman, C. A., Jr. (2005) Designing the Selenium and Vitamin E Cancer Prevention Trial (SELECT) J. Natl. Cancer Inst. 97, 94-102 10.1093/jnci/dji009
102. Lippman, S. M., Klein, E. A., Goodman, P. J., Lucia, M. S., Thompson, I. M., Jr., Ford, L. G., Parnes, H. L., Minasian, L. M., Gaziano, J. M., Hartline, J. A., Parsons, J. K., Bearden, J. D., Crawford, E. D., Goodman, G. E., Claudio, J., Winquist, E., Cook, E. D., Karp, D. D., Walther, P. J., Lieber, M. M., Kristal, A. R., Darke, A. K., Arnold, K. B., Ganz, P. A., Santella, R. M., Albanes, D., Taylor, P. R., Probstfield, J. L., Jagpal, T. J., Crowley, J. J., Meyskens, F. L., Baker, L. H., and Coltman, C. A., Jr. (2009) Effect of selenium and vitamin E on risk of prostate cancer and other cancers: the Selenium and Vitamin E Cancer Prevention Trial (SELECT) JAMA 301, 39-51 10.1001/jama.2008.864
103. Hatfield, D. L. and Gladyshev, V. (2009) The outcome of Selenium and Vitamin E Cancer Prevention Trial (SELECT) reveals the need for better understanding of selenium biology Mol. Interventions 9, 18-21 10.1124/mi.9.1.6
104. Yoo, M. H., Xu, X. M., Carlson, B. A., Patterson, A. D., Gladyshev, V. N., and Hatfield, D. L. (2007) Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication PLoS One 2, e1112 10.1371/journal.pone.0001112
105. Davis, C. D., Tsuji, P. A., and Milner, J. A. (2012) Selenoproteins and cancer prevention Annu. Rev. Nutr. 32, 73-95 10.1146/annurev-nutr-071811-150740
106. Toyokuni, S., Okamoto, K., Yodoi, J., and Hiai, H. (1995) Persistent oxidative stress in cancer FEBS Lett. 358, 1-3 10.1016/0014-5793(94)01368-B
107. Trachootham, D., Alexandre, J., and Huang, P. (2009) Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat. Rev. Drug Discovery 8, 579-591 10.1038/nrd2803
108. Lincoln, D. T., Ali Emadi, E. M., Tonissen, K. F., and Clarke, F. M. (2003) The thioredoxin-thioredoxin reductase system: over-expression in human cancer Anticancer Res. 23, 2425-2433
109. Iwasawa, S., Yamano, Y., Takiguchi, Y., Tanzawa, H., Tatsumi, K., and Uzawa, K. (2011) Upregulation of thioredoxin reductase 1 in human oral squamous cell carcinoma Oncol. Rep. 25, 637-644 10.3892/or.2010.1131
110. Chaudière, J., Courtin, O., and Leclaire, J. (1992) Glutathione oxidase activity of selenocystamine: a mechanistic study Arch. Biochem. Biophys. 296, 328-336 10.1016/0003-9861(92)90580-P
111. Drake, E. N. (2006) Cancer chemoprevention: Selenium as a prooxidant, not an antioxidant Med. Hypotheses 67, 318-322 10.1016/j.mehy.2006.01.058
112. Brodin, O., Eksborg, S., Wallenberg, M., Asker-Hagelberg, C., Larsen, E. H., Mohlkert, D., Lenneby-Helleday, C., Jacobsson, H., Linder, S., Misra, S., and Björnstedt, M. (2015) Pharmacokinetics and toxicity of sodium selenite in the treatment of patients with carcinoma in a phase I clinical trial: The SECAR study Nutrients 7, 4978-4994 10.3390/nu7064978
113. Misra, S., Boylan, M., Selvam, A., Spallholz, J. E., and Björnstedt, M. (2015) Redox-active selenium compounds - from toxicity and cell death to cancer treatment Nutrients 7, 3536-3556 10.3390/nu7053536
114. Oldfield, J. E. (2002) A brief history of selenium research: From alkali disease to prostate cancer (from poison to prevention), J. Anim. Sci. (online edition only). Available at https://www.asas.org/docs/publications/oldfieldhist.pdf?sfvrsn=0.
115. Ching, W.-M. (1984) Occurrence of selenium-containing tRNAs in mouse leukemia cells Proc. Natl. Acad. Sci. U. S. A. 81, 3010-3013 10.1073/pnas.81.10.3010
116. Ching, W.-M. (1986) Characterization of selenium-containing tRNAGlu from Clostridium sticklandii Arch. Biochem. Biophys. 244, 137-146 10.1016/0003-9861(86)90102-5
117. Wittwer, A. J., Tsai, L., Ching, W.-M., and Stadtman, T. C. (1984) Identification and synthesis of a naturally occurring selenonucleoside in bacterial tRNAs: 5-[(methylamino)methyl]-2-selenouridine Biochemistry 23, 4650-4655 10.1021/bi00315a021
118. Wittwer, A. J. and Ching, W.-M. (1989) Selenium-containing tRNA(Glu) and tRNA(Lys) from Escherichia coli: purification, codon specificity and translational activity Biofactors 2, 27-34
119. Romero, H., Zhang, Y., Gladyshev, V. N., and Salinas, G. (2005) Evolution of selenium utilization traits Genome Biol. 6, R66 10.1186/gb-2005-6-8-r66
120. Jones, J. B. and Stadtman, T. C. (1981) Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form J. Biol. Chem. 256, 656-663
121. Axley, M. J., Grahame, D. A., and Stadtman, T. C. (1990) Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component J. Biol. Chem. 265, 18213-18218
122. Gladyshev, V. N., Khangulov, S. V., Axley, M. J., and Stadtman, T. C. (1994) Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 91, 7708-7711 10.1073/pnas.91.16.7708
123. Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C., and Sun, P. D. (1997) Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster Science 275, 1305-1308 10.1126/science.275.5304.1305
124. Khangulov, S. V., Gladyshev, V. N., Dismukes, G. C., and Stadtman, T. C. (1998) Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer Biochemistry 37, 3518-3528 10.1021/bi972177k
125. Yamazaki, S. (1982) A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue J. Biol. Chem. 257, 7926-7929
126. Garcin, E., Vernede, X., Hatchikian, E. C., Volbeda, A., Frey, M., and Fontecilla-Camps, J. C. (1999) The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center Structure 7, 557-566 10.1016/S0969-2126(99)80072-0
127. Lee, B. C., Lobanov, A. V., Marino, S. M., Kaya, A., Seravalli, J., Hatfield, D. L., and Gladyshev, V. N. (2011) A 4-selenocysteine, 2-selenocysteine insertion sequence (SECIS) element methionine sulfoxide reductase from Metridium senile reveals a non-catalytic function of selenocysteines J. Biol. Chem. 286, 18747-18755 10.1074/jbc.M111.229807
128. Yamashita, Y. and Yamashita, M. (2010) Identification of a novel selenium-containing compound, selenoneine, as the predominant chemical form of organic selenium in the blood of bluefin tuna J. Biol. Chem. 285, 18134-18138 10.1074/jbc.C110.106377
129. Yamashita, M., Yamashita, Y., Suzuki, T., Kani, Y., Mizusawa, N., Imamura, S., Takemoto, K., Hara, T., Hossain, M. A., Yabu, T., and Touhata, K. (2013) Selenoneine, a novel selenium-containing compound, mediates detoxification mechanisms against methylmercury accumulation and toxicity in zebrafish embryo Mar. Biotechnol. 15, 559-570 10.1007/s10126-013-9508-1
130. Klein, M., Ouerdane, L., Bueno, M., and Pannier, F. (2011) Identification in human urine and blood of a novel selenium metabolite, Se-methylselenoneine, a potential biomarker of metabolization in mammals of the naturally occurring selenoneine, by HPLC coupled to electrospray hybrid linear ion trap-orbital ion trap MS Metallomics 3, 513-520 10.1039/c0mt00060d
131. Weekley, C. M. and Harris, H. H. (2013) Which form is that? The importance of selenium speciation and metabolism in the prevention and treatment of disease Chem. Soc. Rev. 42, 8870-8894 10.1039/c3cs60272a
132. Lacourciere, G. M., Mihara, H., Kurihara, T., Esaki, N., Stadtman, T. C., and Lacourciere, G. M. (1999) Biosynthesis of selenophosphate BioFactors 10, 237-244 10.1002/biof.5520100222
133. Lacourciere, G. M., Mihara, H., Kurihara, T., Esaki, N., and Stadtman, T. C. (2000) Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate J. Biol. Chem. 275, 23769-23773 10.1074/jbc.M000926200
134. Lacourciere, G. M. and Stadtman, T. C. (2001) Utilization of selenocysteine as a source of selenium for selenophosphate biosynthesis BioFactors 14, 69-74 10.1002/biof.5520140110
135. 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus Proc. Natl. Acad. Sci. U. S. A. 89, 2975-2979 10.1073/pnas.89.7.2975
136. Ehrenreich, A., Forchhammer, K., Tormay, P., Veprek, B., and Böck, A. (1992) Selenoprotein synthesis in E. coli. Purification and characterization of the enzyme catalyzing selenium activation Eur. J. Biochem. 206, 767-773 10.1111/j.1432-1033.1992.tb16983.x
137. Glass, R. S., Singh, W. P., Jung, W., Veres, Z., Scholz, T. D., and Stadtman, T. C. (1993) Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX Biochemistry 32, 12555-12559 10.1021/bi00210a001
138. Forchhammer, K. and Böck, A. (1991) Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence J. Biol. Chem. 266, 6324-6328
139. Xu, X. M., Carlson, B. A., Mix, H., Zhang, Y., Saira, K., Glass, R. S., Berry, M. J., Gladyshev, V. N., and Hatfield, D. L. (2006) Biosynthesis of selenocysteine on its tRNA in eukaryotes PLoS Biol. 5, e4 10.1371/journal.pbio.0050004
140. Xu, X. M., Carlson, B. A., Zhang, Y., Mix, H., Kryukov, G. V., Glass, R. S., Berry, M. J., Gladyshev, V. N., and Hatfield, D. L. (2007) New developments in selenium biochemistry: selenocysteine biosynthesis in eukaryotes and archaea, (2007) Biol. Trace Elem. Res. 119, 234-241 10.1007/s12011-007-8003-9
141. Gammelgaard, B., Jackson, M. I., and Gabel-Jensen, C. (2011) Surveying selenium speciation from soil to cell - forms and transformations Anal. Bioanal. Chem. 399, 1743-1763 10.1007/s00216-010-4212-8
142. Suzuki, K. T., Kurasaki, K., and Suzuki, N. (2007) Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide Biochim. Biophys. Acta, Gen. Subj. 1770, 1053-1061 10.1016/j.bbagen.2007.03.007
143. Meyer, O., Gremer, L., Ferner, R., Ferner, M., Dobbek, H., Gnida, M., Meyer-Klaucke, W., and Huber, R. (2000) The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase Biol. Chem. 381, 865-876 10.1515/BC.2000.108
144. Dobbek, H., Gremer, L., Meyer, O., and Huber, R. (1999) Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine Proc. Natl. Acad. Sci. U. S. A. 96, 8884-8889 10.1073/pnas.96.16.8884
145. Ogra, Y., Ishiwata, K., Takayama, H., Aimi, N., and Suzuki, K. T. (2002) Identification of a novel selenium metabolite, Se-methyl-N-acetylselenohexosamine, in rat urine by high-performance liquid chromatography - inductively coupled plasma mass spectrometry and - electrospray ionization tandem mass spectrometry J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 767, 301-312 10.1016/S1570-0232(01)00581-5
146. Kobayashi, Y., Ogra, Y., Ishiwata, K., Takayama, H., Aimi, N., and Suzuki, K. T. (2002) Selenosugars are key and urinary metabolites for selenium excretion within the required to low-toxic range Proc. Natl. Acad. Sci. U. S. A. 99, 15932-6 10.1073/pnas.252610699
147. McConnell, K. P. and Portman, O. W. (1952) Excretion of dimethyl selenide by the rat J. Biol. Chem. 195, 277-282
148. Byard, J. L. (1969) Trimethyl selenide. A urinary metabolite of selenite Arch. Biochem. Biophys. 130, 556-560 10.1016/0003-9861(69)90070-8
149. Ganther, H. W. (1968) Selenotrisulfides. Formation by the reaction of thiols with selenious acid Biochemistry 7, 2898-2905 10.1021/bi00848a029
150. Andreadou, I., Menge, W., Commandeur, J. N. M., Worthington, E., and Vermeulen, N. (1996) Synthesis of novel Se-substituted selenocysteine derivatives as potential kidney selective prodrugs of biologically active selenol compounds: evaluation of kinetics of beta-elimination reactions in rat renal cytosol J. Med. Chem. 39, 2040-2046 10.1021/jm950750x
151. Rooseboom, M., Vermeulen, N. P. E., Groot, E. J., and Commandeur, J. N. M. (2002) Tissue distribution of cytosolic beta-elimination reactions of selenocysteine Se-conjugates in rat and human Chem.-Biol. Interact. 140, 243-264 10.1016/S0009-2797(02)00039-X
152. Medina, D., Thompson, H., Ganther, H., and Ip, C. (2001) Se-Methylselenocysteine: A new compound for chemoprevention of breast cancer Nutr. Cancer 40, 12-17 10.1207/S15327914NC401-5
153. Ganther, H. E. (1986) Pathways of selenium metabolism including respiratory excretory products Int. J. Toxicol. 5, 1-5 10.3109/10915818609140731
154. Ip, C. and Ganther, H. E. (1990) Activity of methylated forms of selenium in cancer prevention Cancer Res. 50, 1206-1211
155. Ip, C., Thompson, H., Zhu, Z., and Ganther, H. E. (2000) In vitro and in vivo studies of methylseleninic acid: evidence that a monomethylated selenium metabolite is critical for cancer chemoprevention Cancer Res. 60, 2882-2886
156. Ip, C., Hayes, C., Budnick, R. M., and Ganther, H. E. (1991) Chemical form of selenium, critical metabolites, and cancer prevention Cancer Res. 51, 595-600
157. Spallholz, J. E., Palace, V. P., and Reid, T. W. (2004) Methioninase and selenomethionine but not Se-methylselenocysteine generate methylselenol and superoxide in an in vitro chemiluminescent assay: implications for the nutritional carcinostatic activity of selenoamino acids Biochem. Pharmacol. 67, 547-554 10.1016/j.bcp.2003.09.004
158. Hatfield, D. and Diamond, A. (1993) UGA: a split personality in the universal genetic code Trends Genet. 9, 69-70 10.1016/0168-9525(93)90215-4
159. Zinoni, F., Birkmann, A., Stadtman, T. C., and Böck, A. (1986) Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 83, 4650-4654 10.1073/pnas.83.13.4650
160. Chambers, I., Frampton, J., Goldfarb, P., Affara, N., McBain, W., and Harrison, P. R. (1986) The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA EMBO J. 5, 1221-1227
161. Leinfelder, W., Forchhammer, K., Zinoni, F., Sawers, G., Mandrand-Berthelot, M. A., and Böck, A. (1988) Escherichia coli genes whose products are involved in selenium metabolism J. Bacteriol. 170, 540-546
162. Leinfelder, W., Zehelein, E., Mandrand-Berthelot, M. A., and Böck, A. (1988) Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine Nature 331, 723-725 10.1038/331723a0
163. Forchhammer, K., Leinfelder, W., and Böck, A. (1989) Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein Nature 342, 453-456 10.1038/342453a0
164. Berry, M. J., Banu, L., Chen, Y. Y., Mandel, S. J., Kieffer, J. D., Harney, J. W., and Larsen, P. R. (1991) Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′-untranslated region Nature 353, 273-276 10.1038/353273a0
165. Heider, J., Baron, C., and Böck, A. (1992) Coding from a distance: dissection of the mRNA determinants required for the incorporation of selenocysteine into protein EMBO J. 11, 3759-3766
166. Berry, M. J., Banu, L., Harney, J. W., and Larsen, P. R. (1993) Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons EMBO J. 12, 3315-3322
167. Copeland, P. R., Fletcher, J. E., Carlson, B. A., Hatfield, D. L., and Driscoll, D. M. (2000) A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs EMBO J. 19, 306-314 10.1093/emboj/19.2.306
168. Tujebajeva, R. M., Copeland, P. R., Xu, X.-M., Carlson, B. A., Harney, J. W., Driscoll, D. M., Hatfield, D. L., and Berry, M. J. (2000) Decoding apparatus for eukaryotic selenocysteine insertion EMBO Rep. 1, 158-163 10.1093/embo-reports/kvd033
169. Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., and Krol, A. (2000) Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation EMBO J. 19, 4796-4805 10.1093/emboj/19.17.4796
170. Low, S. C. and Berry, M. J. (1996) Knowing when not to stop: selenocysteine incorporation in eukaryotes Trends Biochem. Sci. 21, 203-208 10.1016/S0968-0004(96)80016-8
171. Donovan, J. and Copeland, P. R. (2010) Threading the needle: getting selenocysteine into proteins Antioxid. Redox Signaling 12, 881-892 10.1089/ars.2009.2878
172. Squires, J. E. and Berry, M. J. (2008) Eukaryotic selenoprotein synthesis: mechanistic insight incorporating new factors and new functions for old factors IUBMB Life 60, 232-235 10.1002/iub.38
173. Turanov, A. A., Xu, X. M., Carlson, B. A., Yoo, M. H., Gladyshev, V. N., and Hatfield, D. L. (2011) Biosynthesis of selenocysteine, the 21st amino acid in the genetic code, and a novel pathway for cysteine biosynthesis Adv. Nutr. 2, 122-128 10.3945/an.110.000265
174. Akashi, H. and Gojobori, T. (2002) Metabolic efficiency and amino acid composition in the proteomes of Escherichia coli and Bacillus subtilis Proc. Natl. Acad. Sci. U. S. A. 99, 3695-3700 10.1073/pnas.062526999
175. Wilber, C. G. (1980) Toxicology of selenium: a review Clin. Toxicol. 17, 171-230 10.3109/15563658008985076
176. Shamberger, R. J. (1981) Selenium in the environment Sci. Total Environ. 17, 59-74 10.1016/0048-9697(81)90108-X
177. Girling, C. A. (1984) Selenium in agriculture and the environment Agric., Ecosyst. Environ. 11, 37-65 10.1016/0167-8809(84)90047-1
178. Toppo, S., Vanin, S., Bosello, V., and Tosatto, S. C. E. (2008) Evolutionary and structural insights into the multifaceted glutathione peroxidase (Gpx) superfamily Antioxid. Redox Signaling 10, 1501-1513 10.1089/ars.2008.2057
179. Darras, V. M. and Van Herck, S. L. J. (2012) Iodothyronine deiodinase structure and function: from ascidians to humans J. Endocrinol. 215, 189-206 10.1530/JOE-12-0204
180. Arnér, E. S. (2009) Focus on mammalian thioredoxin reductases - important selenoproteins with versatile functions Biochim. Biophys. Acta, Gen. Subj. 1790, 495-526 10.1016/j.bbagen.2009.01.014
181. Kim, H. Y. (2013) The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions Antioxid. Redox Signaling 19, 958-69 10.1089/ars.2012.5081
182. Lee, B. C., Péterfi, Z., Hoffmann, F. W., Moore, R. E., Kaya, A., Avanesov, A., Tarrago, L., Zhou, Y., Weerapana, E., Fomenko, D. E., Hoffmann, P. R., and Gladyshev, V. N. (2013) MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation Mol. Cell 51, 397-404 10.1016/j.molcel.2013.06.019
183. Lobanov, A. V., Hatfield, D. L., and Gladyshev, V. N. (2008) Selenoproteinless animals: selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis Protein Sci. 17, 176-182 10.1110/ps.073261508
184. Jiang, L., Ni, J., and Liu, Q. (2012) Evolution of selenoproteins in the metazoan BMC Genomics 13, 446 10.1186/1471-2164-13-446
185. Reich, H. J., Wollowitz, S., Trend, J. E., Chow, F., and Wendelborn, D. F. (1978) Syn-elimination of alkyl selenoxides. Side reactions involving selenenic acids, structural and solvent effects on rates J. Org. Chem. 43, 1697-1705 10.1021/jo00403a016
186. Emerson, D. W. and Korniski, T. J. (1969) Substituent effects in the pyrolysis of aryl n-propyl sulfoxides J. Org. Chem. 34, 4115 10.1021/jo01264a076
187. Sugiura, Y., Hojo, Y., Tamai, Y., and Tanaka, H. (1976) Selenium protection against mercury toxicity. Binding of methylmercury by the selenohydryl-containing ligand J. Am. Chem. Soc. 98, 2339-2341 10.1021/ja00424a059
188. Huber, R. E. and Criddle, R. S. (1967) Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analog Arch. Biochem. Biophys. 122, 164-173 10.1016/0003-9861(67)90136-1
189. Pearson, R. G., Sobel, H. R., and Songstad, J. (1968) Nucleophilic reactivity constants toward methyl iodide and trans-dichlorodi(pyridine)platinum(II) J. Am. Chem. Soc. 90, 319-326 10.1021/ja01004a021
190. Halvorsen, A. and Songstad, J. (1978) The reactivity of 2-bromo-1-phenylethanone (phenacyl bromide) toward nucleophilic species J. Chem. Soc., Chem. Commun. 327-328 10.1039/c39780000327
191. Guanti, G., Dell'erba, C., and Spinelli, D. (1970) Cinetica delle reazioni di selenofenossi-dealogenazione di alogeno-nitro-tiofeni Gazz. Chim. Ital. 100, 184-187
192. Hondal, R. J., Nilsson, B. L., and Raines, R. T. (2001) Selenocysteine in native chemical ligation and expressed protein ligation J. Am. Chem. Soc. 123, 5140-5141 10.1021/ja005885t
193. Pinitglang, S., Watts, A. B., Patel, M., Reid, J. D., Noble, M. A., Gul, S., Bokth, A., Naeem, A., Patel, H., Thomas, E. W., Sreedharan, S. K., Verma, C., and Brocklehurst, K. (1997) A classical enzyme active center motif lacks catalytic competence until modulated electrostatically Biochemistry 36, 9968-9982 10.1021/bi9705974
194. Gromer, S., Johansson, L., Bauer, H., Arscott, L. D., Rauch, S., Ballou, D. P., Williams, C. H., Jr., Schirmer, R. H., and Arnér, E. S. (2003) Active sites of thioredoxin reductases: why selenoproteins? Proc. Natl. Acad. Sci. U. S. A. 100, 12618-12623 10.1073/pnas.2134510100
195. Kanzok, S. M., Fechner, A., Bauer, H., Ulschmid, J. K., Müller, H. M., Botella-Munoz, J., Schneuwly, S., Schirmer, R., and Becker, K. (2001) Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster Science 291, 643-646 10.1126/science.291.5504.643
196. Steinmann, D., Nauser, T., and Koppenol, W. H. (2010) Selenium and sulfur in exchange reactions: A comparative study J. Org. Chem. 75, 6696-6699 10.1021/jo1011569
197. Douglas, K. T. (1986) Elimination-addition pathways for thiol esters Acc. Chem. Res. 19, 186-192 10.1021/ar00126a005
198. Cioslowski, J., Piskorz, P., Schimeczek, M., and Boche, G. (1998) Diversity of bonding in methyl ate anions of the first- and second-row elements J. Am. Chem. Soc. 120, 2612-2615 10.1021/ja972564h
199. Ogawa, S., Sato, S., and Furukawa, N. (1992) Kinetic studies on the ligand coupling reactions of tetraphenyl sulfurane, selenurane, and tellurane. Thermal stability for hypervalent chalcogen compounds with four carbon-chalcogen bonds Tetrahedron Lett. 33, 7925-7928 10.1016/S0040-4039(00)74780-0
200. Corey, E. J. and Kim, C. U. (1972) A new and highly effective method for the oxidation of primary and secondary alcohols to carbonyl compounds J. Am. Chem. Soc. 94, 7586-7587 10.1021/ja00776a056
201. Akabori, S., Takanohashi, Y., Aoki, S., and Sato, S. (1991) Correlation between the structure and reactivity of the selenide dihalide of the new reducing reagent NaBH,-R,SeX, on the highly selective reduction of amides. X-ray molecular structure of bis-(2-chloroethyl)selenium dichloride J. Chem. Soc., Perkin Trans. 1 3121-3125 10.1039/P19910003121
202. Melnick, J. G., Yurkerwich, K., and Parkin, J. (2010) On the chalcogenophilicity of mercury: Evidence for a strong Hg-Se Bond in [TmBut]HgSePh and its relevance to the toxicity of mercury J. Am. Chem. Soc. 132, 647-655 10.1021/ja907523x
203. Bachrach, S. M., Demoin, D. W., Luk, M., and Miller, J. V., Jr. (2004) Nucleophilic attack at selenium in diselenides and selenosulfides. A computational study J. Phys. Chem. A 108, 4040-4046 10.1021/jp037972o
204. Corey, E. J. and Seebach, D. (1966) Phenylthiomethyllithium and bis(phenylthio)methyllithium J. Org. Chem. 31, 4097-4099 10.1021/jo01350a052
205. Seebach, D. and Peleties, N. (1972) alpha-Phenylseleno-methyllithiumverbindungen Chem. Ber. 105, 511-520 10.1002/cber.19721050216
206. Reich, H. J., Gudmundsson, B. Ö., Green, D. P., Bevan, M. J., and Reich, I. L. (2002) The role of ate complexes in the lithium-sulfur, lithium-selenium and lithium-tellurium exchange reactions Helv. Chim. Acta 85, 3748-3772 10.1002/1522-2675(200211)85:11<3748::AID-HLCA3748>3.0.CO;2-0
207. Austad, T. (1977) The electrophilic nature of o-nitrobenzenesulfenyl and o-nitrobenzeneselenenyl halides. A kinetic study Acta Chem. Scand. 31A, 93-103 10.3891/acta.chem.scand.31a-0093
208. Gancarz, R. A. and Kice, J. L. (1981) Se-Phenyl areneselenosulfonates: their facile formation and striking chemistry J. Org. Chem. 46, 4899-4906 10.1021/jo00337a015
209. Pleasants, J. C., Guo, W., and Rabenstein, D. L. (1989) A comparative study of the kinetics of selenol/diselenide and thiol/disulfide exchange reactions J. Am. Chem. Soc. 111, 6553-6558 10.1021/ja00199a012
210. Makriyannis, A., Guenther, W. H. H., and Mautner, H. G. (1973) Selenol esters as specific reagents of the acylation of thiol groups J. Am. Chem. Soc. 95, 8403-8406 10.1021/ja00806a033
211. Adams, A. L. and Macmillan, D. (2013) Investigation of peptide thioester formation via N→Se acyl transfer J. Pept. Sci. 19, 65-73 10.1002/psc.2469
212. McGrath, N. A. and Raines, R. T. (2011) Chemoselectivity in chemical biology: acyl transfer reactions with sulfur and selenium Acc. Chem. Res. 44, 752-761 10.1021/ar200081s
213. Mitchell, N. J., Malins, L. R., Liu, X., Thompson, R. E., Chan, B., Radom, L., and Payne, R. J. (2015) Rapid additive-free selenocystine-selenoester peptide ligation J. Am. Chem. Soc. 137, 14011-14014 10.1021/jacs.5b07237
214. Fredericks, G. J. and Hoffmann, P. R. (2015) Selenoprotein K and protein palmitoylation Antioxid. Redox Signaling 23, 854-862 10.1089/ars.2015.6375
215. Krief, A., Dumont, W., and Denis, J. N. (1985) Novel functional group transformations involving alkyl phenyl selenones J. Chem. Soc., Chem. Commun. 571-572 10.1039/c39850000571
216. Shimizu, M., Ando, R., and Kuwajima, I. (1984) Reactions of 3-hydroxyvinyl selenones with alkoxides. Oxetane formation and fragmentation reactions J. Org. Chem. 49, 1230-1238 10.1021/jo00181a020
217. Nylen, P. (1941) The basicity of the arsine oxides and analogous compounds of the groups of nitrogen and sulfur Z. Anorg. Allg. Chem. 246, 227-242 10.1002/zaac.19412460301
218. Bagno, A. and Scorrano, G. (1988) Acid-base properties of organic solvents J. Am. Chem. Soc. 110, 4577-4582 10.1021/ja00222a014
219. Trend, J. E. Physicochemical Studies of Selenoxides and Related Hypervalent Organoselenium Compounds. Nuclear Magnetic Resonance Studies of Organoselenium Compounds, Selenium-77 Chemical Shifts, Ph.D. Thesis, University of Wisconsin-Madison, 1976.
220. Barnard, P. and Woodbridge, D. T. (1959) The oxidation of thio-ethers by selenoxides Chem. Ind. 1603
221. Reich, H. J., Yelm, K. E., and Wollowitz, S. (1983) Kinetics, thermodynamics, and stereochemistry of the allyl sulfoxide-sulfenate and selenoxide-selenenate [2,3] sigmatropic rearrangements J. Am. Chem. Soc. 105, 2503-2504 10.1021/ja00346a082
222. Masilamani, D. and Rogic, M. M. (1978) Organic reactions of sulfur dioxide. 4. A facile regiospecific hydrogen-deuterium exchange in olefins. Consequence of the intermediacy of allylic sulfinic acids in the ene reaction of sulfur dioxide with double bonds J. Am. Chem. Soc. 100, 4634-4635 10.1021/ja00482a072
223. Sharpless, K. B. and Lauer, R. F. (1972) Selenium dioxide oxidation of olefins. Evidence for the intermediacy of allylseleninic acids J. Am. Chem. Soc. 94, 7154-7155 10.1021/ja00775a050
224. Paetzold, R. and Roensch, E. (1965) Alkanseleninsaeurealkylester Z. Anorg. Allg. Chem. 338, 195-198 10.1002/zaac.19653380312
225. Mock, W. L. and McCausland, J. H. (1968) Structure of the diene-selenium dioxide adducts Tetrahedron Lett. 7, 391-392 10.1016/S0040-4039(01)98768-4
226. Heldeweg, R. F. and Hogeveen, H. (1976) 2 + 4) (π + π) and (2 + 4) (n + π) Modes of addition in the reaction between sulfur dioxide and a diene. Kinetic vs. thermodynamic control J. Am. Chem. Soc. 98, 2341-2342 10.1021/ja00424a060
227. Besse, D., Siedler, F., Diercks, T., Kessler, H., and Moroder, L. (1997) The redox potential of selenocystine in unconstrained cyclic peptides Angew. Chem., Int. Ed. Engl. 36, 883-885 10.1002/anie.199708831
228. Metanis, N., Keinan, E., and Dawson, P. E. (2006) Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency J. Am. Chem. Soc. 128, 16684-16691 10.1021/ja0661414
229. Li, F., Lutz, P. B., Pepelyayeva, Y., Arnér, E. S., Bayse, C. A., and Rozovsky, S. (2014) Redox active motifs in selenoproteins Proc. Natl. Acad. Sci. U. S. A. 111, 6976-6981 10.1073/pnas.1319022111
230. Nakamura, N. (1983) A stable sulfenic acid, 9-triptycenesulfenic acid: its isolation and characterization J. Am. Chem. Soc. 105, 7172-7173 10.1021/ja00362a026
231. Goto, K., Holler, M., and Okazaki, R. (1997) Synthesis, structure, and reactions of a sulfenic acid bearing a novel bowl-type substituent: The first synthesis of a stable sulfenic acid by direct oxidation of a thiol J. Am. Chem. Soc. 119, 1460-1461 10.1021/ja962994s
232. Goto, K., Nagahama, M., Mizushima, T., Shimada, K., Kawashima, T., and Okazaki, R. (2001) The first direct oxidative conversion of a selenol to a stable selenenic acid: experimental demonstration of three processes included in the catalytic cycle of glutathione peroxidase Org. Lett. 3, 3569-3572 10.1021/ol016682s
233. Zielinski, Z., Presseau, N., Amorati, R., Valgimigli, L., and Pratt, D. A. (2014) Redox chemistry of selenenic acids and the insight it brings on transition state geometry in the reactions of peroxyl radicals J. Am. Chem. Soc. 136, 1570-1578 10.1021/ja411493t
234. Reich, H. J. and Jasperse, C. P. (1988) Organoselenium chemistry: Preparation and reactions of 2,4,6-tri-t-butylbenzeneselenenic acid J. Org. Chem. 53, 2389-2390 10.1021/jo00245a056
235. Barton, D. H. R., Brewster, A. G., Hui, R. A. H. F., Lester, D. J., Ley, S. V., and Back, T. G. (1978) Oxidation of alcohols using benzeneseleninic anhydride J. Chem. Soc., Chem. Commun. 21, 952-954 10.1039/c39780000952
236. Barton, D. H. R., Finet, J. P., and Martial, T. (1988) Comparative oxidation of phenols with benzeneseleninic anhydride and with benzeneseleninic acid Tetrahedron 44, 6397-6406 10.1016/S0040-4020(01)89827-6
237. Back, T. G. and Back, T. G. (2007) Benzeneseleninic acid e-EROS Encyclopedia of Reagents for Organic Synthesis 1-8 10.1002/9780470842898.rb016.pub2
238. Gancarz, R. A. and Kice, J. L. (1980) The reaction of sulfinic acids with benzeneseleninic acid Tetrahedron Lett. 21, 1697-1700 10.1016/S0040-4039(00)77813-0
239. Gould, E. S. and McCullough, J. D. (1951) The dissociation constants of some monosubstituted benzeneseleninic acids. II A new synthesis of diaryl diselenides J. Am. Chem. Soc. 73, 1109-1112 10.1021/ja01147a067
240. De Filippo, D. and Momicchioli, F. A. (1969) Study of benzenesulfinic and seleninic acids. Determination and theoretical interpretation of pK Tetrahedron 25, 5733-5744 10.1016/S0040-4020(01)83080-5
241. Abdo, M. and Knapp, S. (2008) Biomimetic seleninates and selenonates J. Am. Chem. Soc. 130, 9234-9235 10.1021/ja8034448
242. Bell, I. M., Fisher, M. L., Wu, Z. P., and Hilvert, D. (1993) Kinetic studies on the peroxidase activity of selenosubtilisin Biochemistry 32, 3754-3762 10.1021/bi00065a030
243. Ruggles, E. L., Snider, G. W., and Hondal, R. J. (2012) Chemical basis for the use of selenocysteine. In Selenium: Its Molecular Biology and Role in Human Health, 3 rd ed. (Hatfield, D. L., Berry, M. J., and Gladyshev, V. N., Eds.) pp 73-83, Springer, New York, 2012.
244. Wu, Z. P. and Hilvert, D. (1990) Selenosubtilisin as a glutathione peroxidase mimic J. Am. Chem. Soc. 112, 5647-5648 10.1021/ja00170a043
245. Kice, J. L. and Lee, T. W. S. (1978) Oxidation-reduction reactions of organoselenium compounds. 1. Mechanism of the reaction between seleninic acids and thiols J. Am. Chem. Soc. 100, 5094-5102 10.1021/ja00484a031
246. Nauser, T., Steinmann, D., Grassi, G., and Koppenol, W. H. (2014) Why selenocysteine replaces cysteine in thioredoxin reductase: a radical hypothesis Biochemistry 53, 5017-5022 10.1021/bi5003376
247. Axley, M. J., Böck, A., and Stadtman, T. C. (1991) Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium Proc. Natl. Acad. Sci. U. S. A. 88, 8450-8454 10.1073/pnas.88.19.8450
248. Berry, M. J., Maia, A. L., Kieffer, J. D., Harney, J. W., and Larsen, P. R. (1992) Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation Endocrinology 131, 1848-1852 10.1210/endo.131.4.1396330
249. Rocher, C., Lalanne, J. L., and Chaudière, J. (1992) Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase Eur. J. Biochem. 205, 955-960 10.1111/j.1432-1033.1992.tb16862.x
250. Maiorino, M., Aumann, K. D., Brigelius-Flohé, R., Doria, D., van den Heuvel, J., McCarthy, J., Roveri, A., Ursini, F., and Flohé, L. (1995) Probing the presumed catalytic triad of selenium-containing peroxidases by mutational analysis of phospholipid hydroperoxide glutathione peroxidase (PHGPx) Biol. Chem. Hoppe-Seyler 376, 651-660 10.1515/bchm3.1995.376.11.651
251. Hazebrouck, S., Camoin, L., Faltin, Z., Strosberg, A. D., and Eshdat, Y. (2000) Substituting selenocysteine for catalytic cysteine 41 enhances enzymatic activity of plant phospholipid hydroperoxide glutathione peroxidase expressed in Escherichia coli J. Biol. Chem. 275, 28715-28721 10.1074/jbc.M004985200
252. Kim, H. Y., Fomenko, D. E., Yoon, Y. E., and Gladyshev, V. N. (2006) Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases Biochemistry 45, 13697-13704 10.1021/bi0611614
253. Kim, H. Y. and Gladyshev, V. N. (2005) Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases PLoS Biol. 3, e375 10.1371/journal.pbio.0030375
254. Lacourciere, G. M. and Stadtman, T. C. (1999) Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 96, 44-48 10.1073/pnas.96.1.44
255. Casi, G., Roelfes, G., and Hilvert, D. (2008) Selenoglutaredoxin as a glutathione peroxidase mimic ChemBioChem 9 (10) 1623-1631 10.1002/cbic.200700745
256. Boschi-Muller, S., Muller, S., Van Dorsselaer, A., Böck, A., and Branlant, G. (1998) Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity FEBS Lett. 439, 241-245 10.1016/S0014-5793(98)01377-5
257. Ding, L., Liu, Z., Zhu, Z., Luo, G., Zhao, D., and Ni, J. (1998) Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic Biochem. J. 332, 251-255 10.1042/bj3320251
258. Liu, J.-Q., Jiang, M.-S., Luo, G.-M., Yan, G.-L., and Shen, J.-C. (1998) Conversion of trypsin into a selenium-containing enzyme by using chemical mutation Biotechnol. Lett. 20, 693-696 10.1023/A:1005378709179
259. Sun, Y., Li, T., Chen, H., Zhang, K., Zheng, K., Mu, Y., Yan, G., Li, W., Shen, J., and Luo, G. (2004) Selenium-containing 15-mer peptides with high glutathione peroxidase-like activity J. Biol. Chem. 279, 37235-37240 10.1074/jbc.M403032200
260. Ren, X., Jemth, P., Board, P. G., Luo, G., Mannervik, B., Liu, J., Zhang, K., and Shen, J. (2002) A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase Chem. Biol. 9, 789-94 10.1016/S1074-5521(02)00167-9
261. Poole, L. B. (2007) The catalytic mechanism of peroxiredoxins Subcell. Biochem. 44, 61-81 10.1007/978-1-4020-6051-9-4
262. Biteau, B., Labarre, J., and Toledano, M. B. (2003) ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425, 980-984 10.1038/nature02075
263. Snider, G. W., Ruggles, E. L., Khan, N., and Hondal, R. J. (2013) Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: Comparison of selenium and sulfur enzymes Biochemistry 52, 5472-5481 10.1021/bi400462j
264. Dimastrogiovanni, D., Anselmi, M., Miele, A. E., Boumis, G., Petersson, L., Angelucci, F., Nola, A. D., Brunori, M., and Bellelli, A. (2010) Combining crystallography and molecular dynamics: the case of Schistosoma mansoni phospholipid glutathione peroxidase Proteins: Struct., Funct., Genet. 78, 259-270 10.1002/prot.22536
265. Orian, L., Mauri, P., Roveri, A., Toppo, S., Benazzi, L., Bosello-Travain, V., De Palma, A., Maiorino, M., Miotto, G., Zaccarin, M., Polimeno, A., Flohé, L., and Ursini, F. (2015) Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study Free Radical Biol. Med. 87, 1-14 10.1016/j.freeradbiomed.2015.06.011
266. Reich, H. J. and Jasperse, C. P. (1987) Organoselenium chemistry. Redox chemistry of selenocysteine model systems J. Am. Chem. Soc. 109, 5549-5553 10.1021/ja00252a055
267. Kice, J. L. and Kutateladze, A. G. (1993) The markedly enhanced basicity of selenenamides vs sulfenamides and the mechanism of the methanolysis of o-nitro- and 2,4,6-tri-tert-butylbenzeneselenenamides J. Org. Chem. 58, 917-923 10.1021/jo00056a026
268. Syed, R., Wu, Z. P., Hogle, J. M., and Hilvert, D. (1993) Crystal structure of selenosubtilisin at 2.0-Å resolution Biochemistry 32, 6157-6164 10.1021/bi00075a007
269. 77Se NMR spectroscopy J. Am. Chem. Soc. 114, 8573-8579 10.1021/ja00048a033
270. Maller, C., Schröder, E., and Eaton, P. (2011) Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: studies with a novel anti-dimedone sulfenic acid antibody Antioxid. Redox Signaling 14, 49-60 10.1089/ars.2010.3149
271. Teixeira, M., Fauque, G., Moura, I., Lespinat, P. A., Berlier, Y., Prickril, B., Peck, H. D., Jr., Xavier, A. V., Le Gall, J., and Moura, J. J. (1987) Nickel-[iron-sulfur]-selenium-containing hydrogenases from Desulfovibrio baculatus (DSM 1743). Redox centers and catalytic properties Eur. J. Biochem. 167, 47-58 10.1111/j.1432-1033.1987.tb13302.x
272. Choudhury, S. B., Pressler, M. A., Mirza, S. A., Day, R. O., and Maroney, M. J. (1994) Structure and redox chemistry of analogous nickel thiolato and selenolato complexes: Implications for the nickel sites in hydrogenases Inorg. Chem. 33, 4831-4839 10.1021/ic00100a005
273. Maroney, M. J., Choudhury, S. B., Allan, C. B., and Davidson, G. (1998) The role of selenocysteine in Ni, Fe hydrogenases: Biophysical and synthetic model studies Phosphorus, Sulfur Silicon Relat. Elem. 136, 361-366 10.1080/10426509808545962
274. Parkin, A., Goldet, G., Cavazza, C., Fontecilla-Camps, J. C., and Armstrong, F. A. (2008) The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum J. Am. Chem. Soc. 130, 13410-13416 10.1021/ja803657d
275. Marques, M. C., Coelho, R., De Lacey, A. L., Pereira, I. A., and Matias, P. M. (2010) The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated"state J. Mol. Biol. 396, 893-907 10.1016/j.jmb.2009.12.013
276. Sivaramakrishnan, S., Ouellet, H., Du, J., McLean, K. J., Medzihradszky, K. F., Dawson, J. H., Munro, A. W., and Ortiz de Montellano, P. R. (2011) A novel intermediate in the reaction of seleno CYP119 with m-chloroperbenzoic acid Biochemistry 50, 3014-3024 10.1021/bi101728y
277. Eckenroth, B. E., Rould, M. A., Hondal, R. J., and Everse, S. J. (2007) Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases Biochemistry 46, 4694-4705 10.1021/bi602394p
278. Eckenroth, B. E., Harris, K., Turanov, A. A., Gladyshev, V. N., Raines, R. T., and Hondal, R. J. (2006) Semisynthesis and characterization of mammalian thioredoxin reductase Biochemistry 45, 5158-5170 10.1021/bi0517887
279. Berner, R. A., Vandenbrooks, J. M., and Ward, P. D. (2007) Evolution. Oxygen and evolution Science 316, 557-558 10.1126/science.1140273