메뉴 건너뛰기




Volumn 18, Issue 13, 2013, Pages 1675-1689

Selenocysteine in thiol/disulfide-like exchange reactions

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; OXIDOREDUCTASE; PEROXIDASE; SELENIUM; SELENOCYSTEINE; SULFUR; THIOL;

EID: 84875729310     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.5013     Document Type: Review
Times cited : (142)

References (91)
  • 1
    • 0242413235 scopus 로고    scopus 로고
    • Kinetic Characterization of the Chemical Steps Involved in the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis
    • DOI 10.1074/jbc.M307471200
    • Antoine M, Boschi-Muller S, and Branlant G. Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitides. J Biol Chem 278: 45352-45357, 2003. (Pubitemid 37432671)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45352-45357
    • Antoine, M.1    Boschi-Muller, S.2    Branlant, G.3
  • 2
    • 77952563903 scopus 로고    scopus 로고
    • Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine
    • Arnér ES. Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine. Exp Cell Res 316: 1296-1303, 2010.
    • (2010) Exp Cell Res , vol.316 , pp. 1296-1303
    • Arnér, E.S.1
  • 3
    • 0031819753 scopus 로고    scopus 로고
    • Reduction of methionine selenoxide to selenomethionine by glutathione
    • DOI 10.1006/abbi.1997.0462
    • Assmann A, Briviba K, and Sies H. Reduction of methionine selenoxide to selenomethionine by glutathione. Arch Biochem Biophys 349: 201-203, 1998. (Pubitemid 28368407)
    • (1998) Archives of Biochemistry and Biophysics , vol.349 , Issue.1 , pp. 201-203
    • Assmann, A.1    Briviba, K.2    Sies, H.3
  • 4
    • 0034727069 scopus 로고    scopus 로고
    • The twenty-first amino acid
    • Atkins JF and Gesteland RF. The twenty-first amino acid. Nature 407: 463-465, 2000.
    • (2000) Nature , vol.407 , pp. 463-465
    • Atkins, J.F.1    Gesteland, R.F.2
  • 5
    • 2442690474 scopus 로고    scopus 로고
    • Nucleophilic attack at selenium in diselenides and selenosulfides: A computational study
    • Bachrach SM, Demoin DW, Luk M, and Miller JV, Jr. Nucleophilic attack at selenium in diselenides and selenosulfides: a computational study. J Phys Chem A 108: 4040-4046, 2004.
    • (2004) J Phys Chem A , vol.108 , pp. 4040-4046
    • Bachrach, S.M.1    Demoin, D.W.2    Luk, M.3    Miller Jr., J.V.4
  • 6
    • 0036910439 scopus 로고    scopus 로고
    • Trends in selenium biochemistry
    • DOI 10.1039/b205802m
    • Birringer M, Pilawa P, and Flohe F. Trends in selenium biochemistry. Nat Prod Rep 19: 693-718, 2002. (Pubitemid 36029227)
    • (2002) Natural Product Reports , vol.19 , Issue.6 , pp. 693-718
    • Birringer, M.1    Pilawa, S.2    Flohe, L.3
  • 8
    • 12844275002 scopus 로고    scopus 로고
    • The enzymology and biochemistry of methionine sulfoxide reductases
    • DOI 10.1016/j.bbapap.2004.09.016, PII S1570963904002535, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Boschi-Muller S, Olry A, Antoine M, and Branlant G. The enzymology and biochemistry of methionine sulfoxide reductases. Biochim Biophys Acta 1703: 231-238, 2005. (Pubitemid 40170446)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 231-238
    • Boschi-Muller, S.1    Olry, A.2    Antoine, M.3    Branlant, G.4
  • 10
    • 33847020014 scopus 로고    scopus 로고
    • Selenocysteine versus cysteine reactivity: A theoretical study of their oxidation by hydrogen peroxide
    • Cardey B and Enescu M. Selenocysteine versus cysteine reactivity: a theoretical study of their oxidation by hydrogen peroxide. J Phys Chem A 111: 673-638, 2007.
    • (2007) J Phys Chem A , vol.111 , pp. 673-638
    • Cardey, B.1    Enescu, M.2
  • 12
    • 48649085619 scopus 로고    scopus 로고
    • Selenoglutaredoxin as a glutathione peroxidase mimic
    • Casi G, Roelfes G, and Hilvert D. Selenoglutaredoxin as a glutathione peroxidase mimic. Chem Bio Chem 9: 1623-1631, 2008.
    • (2008) Chem Bio Chem , vol.9 , pp. 1623-1631
    • Casi, G.1    Roelfes, G.2    Hilvert, D.3
  • 14
    • 0001100392 scopus 로고
    • The relation between the structure of organic halides and the speeds of their reaction with inorganic iodides III: The influence of unsaturated groups
    • Conant JB, Kirner WR, and Hussey RE. The relation between the structure of organic halides and the speeds of their reaction with inorganic iodides III: the influence of unsaturated groups. J Am Chem Soc 47: 488-501, 1925.
    • (1925) J Am Chem Soc , vol.47 , pp. 488-501
    • Conant, J.B.1    Kirner, W.R.2    Hussey, R.E.3
  • 15
    • 0000195317 scopus 로고
    • The relative nucleophilic character of several mercaptans toward ethylene oxide
    • Danehy JP and Noel CJ. The relative nucleophilic character of several mercaptans toward ethylene oxide. J Am Chem Soc 82: 2511-2515, 1960.
    • (1960) J Am Chem Soc , vol.82 , pp. 2511-2515
    • Danehy, J.P.1    Noel, C.J.2
  • 16
    • 0009761277 scopus 로고
    • The alkaline decomposition of organic disulfides. IV. A limitation on the use of Ellman's Reagent, 2,2¢-Dinitro-5,5¢-dithiodibenzoic acid
    • Danehy JP, Elia VJ, and Lavelle CJ. The alkaline decomposition of organic disulfides. IV. A limitation on the use of Ellman's Reagent, 2,2¢-Dinitro-5,5¢-dithiodibenzoic acid. J Org Chem 36: 1003-1005, 1971.
    • (1971) J Org Chem , vol.36 , pp. 1003-1005
    • Danehy, J.P.1    Elia, V.J.2    Lavelle, C.J.3
  • 18
    • 34548072585 scopus 로고    scopus 로고
    • r thioredoxin reductase by protein engineering and semisynthesis
    • DOI 10.1021/bi7004812
    • Eckenroth BE, Lacey BM, Lothrop AP, Harris KM, and Hondal RJ. Investigation of the C-terminal redox center of high Mr thioredoxin reductases by protein engineering and semisynthesis. Biochemistry 46: 9472-9483, 2007. (Pubitemid 47291954)
    • (2007) Biochemistry , vol.46 , Issue.33 , pp. 9472-9483
    • Eckenroth, B.E.1    Lacey, B.M.2    Lothrop, A.P.3    Harris, K.M.4    Hondal, R.J.5
  • 19
    • 34247479503 scopus 로고    scopus 로고
    • Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases
    • DOI 10.1021/bi602394p
    • Eckenroth BE, Rould MA, Hondal RJ, and Everse SJ. Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases. Biochemistry 46: 4694-4705, 2007. (Pubitemid 46651193)
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4694-4705
    • Eckenroth, B.E.1    Rould, M.A.2    Hondal, R.J.3    Everse, S.J.4
  • 20
    • 0020775636 scopus 로고
    • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
    • Epp O, Ladenstein R, and Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur J Biochem 133: 51-69, 1983.
    • (1983) Eur J Biochem , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 21
    • 44349098103 scopus 로고    scopus 로고
    • Synthesis of peptide substrates forl mammalian thioredoxin reductase
    • DOI 10.1002/psc.961
    • Flemer SJ, Lacey BM, and Hondal RJ. Synthesis of peptide substrates for mammalian thioredoxin reductase. J Pept Sci 14: 637-47, 2008. (Pubitemid 351736460)
    • (2008) Journal of Peptide Science , vol.14 , Issue.5 , pp. 637-647
    • Flemer Jr., S.1    Lacey, B.M.2    Hondal, R.J.3
  • 22
    • 79960322216 scopus 로고    scopus 로고
    • Crystal structure of the human thioredoxin reductasethioredoxin complex
    • Fritz-Wolf K, Kehr S, Stumpf M, Rahlfs S, and Becker K. Crystal structure of the human thioredoxin reductasethioredoxin complex. Nat Commun 2: 383, 2011.
    • (2011) Nat Commun , vol.2 , pp. 383
    • Fritz-Wolf, K.1    Kehr, S.2    Stumpf, M.3    Rahlfs, S.4    Becker, K.5
  • 23
    • 0014196757 scopus 로고
    • The chemistry of flavins and flavoproteins. The reaction of dihydrolipoic acid with flavins
    • Gascoigne IM and Radda GK. The chemistry of flavins and flavoproteins. The reaction of dihydrolipoic acid with flavins. Biochim Biophys Acta 131: 498-507, 1967.
    • (1967) Biochim Biophys Acta , vol.131 , pp. 498-507
    • Gascoigne, I.M.1    Radda, G.K.2
  • 24
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63: 69-172, 1990.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 25
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • Gilbert HF. Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol 251: 8-28, 1995.
    • (1995) Methods Enzymol , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 26
    • 17444409795 scopus 로고    scopus 로고
    • Thiol/disulfide exchange and redox potentials of proteins
    • edited by Lenaz G and Milazzo G. Basel, Switzerland: Birhauser
    • Gilbert HF. Thiol/disulfide exchange and redox potentials of proteins. In: Bioelectrochemistry of Biomacromolecules, edited by Lenaz G and Milazzo G. Basel, Switzerland: Birhauser, 1997, pp. 256-324.
    • (1997) Bioelectrochemistry of Biomacromolecules , pp. 256-324
    • Gilbert, H.F.1
  • 27
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
    • DOI 10.1073/pnas.93.12.6146
    • Gladyshev VN, Jeang KT, and Stadtman TC. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci U S A 93: 6146-6151, 1996. (Pubitemid 26190818)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.12 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.-T.2    Stadtman, T.C.3
  • 28
    • 0027957511 scopus 로고
    • Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme
    • DOI 10.1073/pnas.91.1.232
    • Gladyshev VN, Khangulov SV, and Stadtman TC. Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme. Proc Natl Acad Sci U S A 91: 232-236, 1994. (Pubitemid 24018678)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.1 , pp. 232-236
    • Gladyshev, V.N.1    Khangulov, S.V.2    Stadtman, T.C.3
  • 30
    • 11944264414 scopus 로고
    • Ribonuclease revisited: Catalysis via the classical general acid-base mechanism or a triester-like mechanism?
    • Herschlag D. Ribonuclease revisited: catalysis via the classical general acid-base mechanism or a triester-like mechanism? J Am Chem Soc 116: 11631-11635, 1994.
    • (1994) J Am Chem Soc , vol.116 , pp. 11631-11635
    • Herschlag, D.1
  • 31
    • 0025912639 scopus 로고
    • The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame
    • Hill KE, Lloyd RS, Yang JG, Read R, and Burk RF. The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame. J Biol Chem 266: 10050-10053, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 10050-10053
    • Hill, K.E.1    Lloyd, R.S.2    Yang, J.G.3    Read, R.4    Burk, R.F.5
  • 32
    • 27744456247 scopus 로고    scopus 로고
    • Incorporation of selenocysteine into proteins using peptide ligation
    • DOI 10.2174/0929866054864319
    • Hondal RJ. Incorporation of selenocysteine into proteins using peptide ligation. Prot Pept Lett 12: 757-764, 2005. (Pubitemid 41634854)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.8 , pp. 757-764
    • Hondal, R.J.1
  • 33
    • 0034808792 scopus 로고    scopus 로고
    • Selenocysteine in native chemical ligation and expressed protein ligation
    • DOI 10.1021/ja005885t
    • Hondal RJ, Nilsson BL, and Raines RT. Selenocysteine in native chemical ligation and expressed protein ligation. J Am Chem Soc 123: 5140-5141, 2001. (Pubitemid 32905687)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.21 , pp. 5140-5141
    • Hondal, R.J.1    Nilsson, B.L.2    Raines, R.T.3
  • 34
    • 79959345933 scopus 로고    scopus 로고
    • Differing views of the role of selenium in thioredoxin reductase
    • Hondal RJ and Ruggles EL. Differing views of the role of selenium in thioredoxin reductase. Amino Acids 41: 73-89, 2011.
    • (2011) Amino Acids , vol.41 , pp. 73-89
    • Hondal, R.J.1    Ruggles, E.L.2
  • 35
    • 0003184034 scopus 로고    scopus 로고
    • 4): Relationship between HEAr acidity and enthalpy of reaction
    • 2 to (PMe3)4Ru(C2H4): relationship between HEAr acidity and enthalpy of reaction. Organometallics 17: 3516-3521, 1998. (Pubitemid 128572454)
    • (1998) Organometallics , vol.17 , Issue.16 , pp. 3516-3521
    • Huang, J.1    Li, C.2    Nolan, S.P.3    Petersen, J.L.4
  • 36
    • 0014143854 scopus 로고
    • Comparison of the chemical properties of selenocysteine and selenocystine and their sulfur analogs
    • Huber RE and Criddle RS. Comparison of the chemical properties of selenocysteine and selenocystine and their sulfur analogs. Arch Biochem Biophys 122: 164-173, 1967.
    • (1967) Arch Biochem Biophys , vol.122 , pp. 164-173
    • Huber, R.E.1    Criddle, R.S.2
  • 38
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and Selenium: The Role of Oxidation State in Protein Structure and Function
    • DOI 10.1002/anie.200300573
    • Jacob C, Giles GI, Giles NM, and Sies H. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew Chem Int Ed Engl 42: 4742-4758, 2003. (Pubitemid 37314599)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.39 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 40
    • 1542313980 scopus 로고    scopus 로고
    • Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases
    • DOI 10.1091/mbc.E03-08-0629
    • Kim HY and Gladyshev VN. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell 15: 1055-1064, 2004. (Pubitemid 38316216)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1055-1064
    • Kim, H.-Y.1    Gladyshev, V.N.2
  • 41
    • 29144494461 scopus 로고    scopus 로고
    • Different catalytic mechanisms in mammalian selenocysteine-and cysteine-containing methionine-R-sulfoxide reductases
    • Kim HY and Gladyshev VN. Different catalytic mechanisms in mammalian selenocysteine-and cysteine-containing methionine-R-sulfoxide reductases. PloS Biology 3: e375, 2005.
    • (2005) PloS Biology , vol.3
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 42
    • 33751220854 scopus 로고    scopus 로고
    • Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases
    • DOI 10.1021/bi0611614
    • Kim HY, Fomenko DE, Yoon YE, and Gladyshev VN. Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases. Biochemistry 45: 13697-13704, 2006. (Pubitemid 44788740)
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13697-13704
    • Kim, H.-Y.1    Fomenko, D.E.2    Yoon, Y.-E.3    Gladyshev, V.N.4
  • 43
    • 56649097337 scopus 로고    scopus 로고
    • Reduction of L-methionine selenoxide to seleno-L-methione by endogenous thiols, ascorbic acid, or methimazole
    • Krause RJ and Elfarra AA. Reduction of L-methionine selenoxide to seleno-L-methione by endogenous thiols, ascorbic acid, or methimazole. Biochem Pharmacol 77: 134-140, 2009.
    • (2009) Biochem Pharmacol , vol.77 , pp. 134-140
    • Krause, R.J.1    Elfarra, A.A.2
  • 44
    • 0035826594 scopus 로고    scopus 로고
    • Mechanism of phosphatidylinositol-specific phospholipase C: Origin of unusually high nonbridging thio effects
    • DOI 10.1021/bi002372q
    • Kravchuk AV, Zhao L, Kubiak RJ, Bruzik KS, and Tsai M-D. Mechanism of phosphatidylinositol-specific phospholipase C: origin of unusually high nonbridging thio effects. Biochemistry 40: 5433-5439, 2001. (Pubitemid 32458244)
    • (2001) Biochemistry , vol.40 , Issue.18 , pp. 5433-5439
    • Kravchuk, A.V.1    Zhao, L.2    Kubiak, R.J.3    Bruzik, K.S.4    Tsai, M.-D.5
  • 47
    • 57049139414 scopus 로고    scopus 로고
    • Selenium in thioredoxin reductase: A mechanistic perspective
    • Lacey BM, Flemer SJ, Eckenroth BE, and Hondal RJ. Selenium in thioredoxin reductase: a mechanistic perspective. Biochemistry 47: 12810-12821, 2008.
    • (2008) Biochemistry , vol.47 , pp. 12810-12821
    • Lacey, B.M.1    Flemer, S.J.2    Eckenroth, B.E.3    Hondal, R.J.4
  • 48
    • 79956318386 scopus 로고    scopus 로고
    • A 4-selenocysteine, 2-selenocysteine insertion sequence (SECIS) element methionine sulfoxide reductase from Metridium senile reveals a non-catalytic function of selenocysteines
    • Lee BC, Lobanov AV, Marino SM, Kaya A, Seravalli J, Hatfield DL, and Gladyshev VN. 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, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 18747-18755
    • Lee, B.C.1    Lobanov, A.V.2    Marino, S.M.3    Kaya, A.4    Seravalli, J.5    Hatfield, D.L.6    Gladyshev, V.N.7
  • 50
    • 67650092048 scopus 로고    scopus 로고
    • No selenium required: Reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue
    • Lothrop AP, Ruggles EL, and Hondal RJ. No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue. Biochemistry 48: 6213-6223, 2009.
    • (2009) Biochemistry , vol.48 , pp. 6213-6223
    • Lothrop, A.P.1    Ruggles, E.L.2    Hondal, R.J.3
  • 51
    • 0037811713 scopus 로고    scopus 로고
    • Loss of selenium from selenoproteins: Conversion of selenocysteine to dehydroalanine in vitro
    • DOI 10.1016/S1044-0305(03)00141-7
    • Ma S, Caprioli RM, Hill KE, and Burk RF. Loss of selenium from selenoproteins: conversion of selenocysteine to dehydroalanine in vitro. J Am Soc Mass Spectrom 14: 593-600, 2003. (Pubitemid 36870967)
    • (2003) Journal of the American Society for Mass Spectrometry , vol.14 , Issue.6 , pp. 593-600
    • Ma, S.1    Caprioli, R.M.2    Hill, K.E.3    Burk, R.F.4
  • 53
    • 83455242984 scopus 로고    scopus 로고
    • Site-specific pKa determination of selenocysteine residues in selenovasopressin by using 77Se NMR spectroscopy
    • Mehdi M, Morgenstern D, King GF, Alewood PF, and Muttenthaler M. Site-specific pKa determination of selenocysteine residues in selenovasopressin by using 77Se NMR spectroscopy. Angew Chem Int Ed 50: 11952-11955, 2011.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 11952-11955
    • Mehdi, M.1    Morgenstern, D.2    King, G.F.3    Alewood, P.F.4    Muttenthaler, M.5
  • 55
    • 33845940127 scopus 로고    scopus 로고
    • Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency
    • DOI 10.1021/ja0661414
    • Metanis N, Keinan E, and Dawson PE. Synthetic selenoglutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency. J Am Chem Soc 128: 16684-16691, 2006. (Pubitemid 46032748)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.51 , pp. 16684-16691
    • Metanis, N.1    Keinan, E.2    Dawson, P.E.3
  • 56
    • 0034413683 scopus 로고    scopus 로고
    • Synthetic organoselenium compounds as antioxidants: Glutathione peroxidase activity
    • Mugesh G and Sing HB. Synthetic organoselenium compounds as antioxidants: glutathione peroxidase activity. Chem Soc Rev 29: 347-357, 2000.
    • (2000) Chem Soc Rev , vol.29 , pp. 347-357
    • Mugesh, G.1    Sing, H.B.2
  • 57
    • 36148986798 scopus 로고    scopus 로고
    • Characterization of the amino acids from Neisseria meningitidis methionine sulfoxide reductase B involved in the chemical catalysis and substrate specificity of the reductase step
    • DOI 10.1074/jbc.M704730200
    • Neiers F, Sonkaria S, Olry A, Boschi-Muller S, and Branlant G. Characterization of the amino acids from Neisseria meningitidis methionine sulfoxide reductase B involved in the chemical catalysis and substrate specificity of the reductase step. J Biol Chem 282: 32397-32405, 2007. (Pubitemid 350106432)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 32397-32405
    • Neiers, F.1    Sonkaria, S.2    Olry, A.3    Boschi-Muller, S.4    Branlant, G.5
  • 58
    • 4444284939 scopus 로고    scopus 로고
    • Kinetic characterization of the catalytic mechanism of methionine sulfoxide reductase B from Neisseria meningitidis
    • DOI 10.1021/bi049306z
    • Olry A, Boschi-Muller S, and Branlant G. Kinetic characterization of the catalytic mechanism of methionine sulfoxide reductase B from Neisseria meningitides. Biochemistry 43: 11616-11622, 2004. (Pubitemid 39186983)
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11616-11622
    • Olry, A.1    Boschi-Muller, S.2    Branlant, G.3
  • 59
    • 33947332005 scopus 로고
    • Application of the principle of hard and soft acids and bases to organic chemistry
    • Pearson RG and Songstad J. Application of the principle of hard and soft acids and bases to organic chemistry. J Am Chem Soc 89: 1827-1836, 1967.
    • (1967) J Am Chem Soc , vol.89 , pp. 1827-1836
    • Pearson, R.G.1    Songstad, J.2
  • 60
    • 33947323024 scopus 로고
    • Nucleophilic reactivity constants toward methyl iodide and trans-[Pt(py)2Cl2]
    • Pearson RG and Songstad J. Nucleophilic reactivity constants toward methyl iodide and trans-[Pt(py)2Cl2]. J Am Chem Soc 90: 319-326, 1968.
    • (1968) J Am Chem Soc , vol.90 , pp. 319-326
    • Pearson, R.G.1    Songstad, J.2
  • 62
    • 0001586953 scopus 로고
    • A comparative study of the kinetics of selenol/diselenide and thiol/disulfide exchange reactions
    • Pleasants JC, Guo W, and Rabenstein DL. A comparative study of the kinetics of selenol/diselenide and thiol/disulfide exchange reactions. J Am Chem Soc 111: 6553-6558, 1989.
    • (1989) J Am Chem Soc , vol.111 , pp. 6553-6558
    • Pleasants, J.C.1    Guo, W.2    Rabenstein, D.L.3
  • 63
    • 38749094500 scopus 로고    scopus 로고
    • The catalytic mechanism of peroxiredoxins
    • Poole LB. The catalytic mechanism of peroxiredoxins. Subcell Biochem 44: 61-81, 2007.
    • (2007) Subcell Biochem , vol.44 , pp. 61-81
    • Poole, L.B.1
  • 64
    • 2442661374 scopus 로고
    • Nuclear magnetic resonance study of the kinetics of the penicillamine/ bis(penicillamine) selenide symmetrical exchange reaction
    • Rabenstein DR, Scott TM, and Geo W. Nuclear magnetic resonance study of the kinetics of the penicillamine/ bis(penicillamine) selenide symmetrical exchange reaction. J Org Chem 56: 4176-4181, 1991.
    • (1991) J Org Chem , vol.56 , pp. 4176-4181
    • Rabenstein, D.R.1    Scott, T.M.2    Geo, W.3
  • 66
    • 33845283525 scopus 로고
    • Organoselenium chemistry: Redox chemistry of selenocysteine model systems
    • Reich HJ and Jasperse CP. Organoselenium chemistry: redox chemistry of selenocysteine model systems. J Am Chem Soc 109: 5549-5551, 1987.
    • (1987) J Am Chem Soc , vol.109 , pp. 5549-5551
    • Reich, H.J.1    Jasperse, C.P.2
  • 67
    • 0026587399 scopus 로고
    • Purification and properties of a recombinant sulfur analog of murine seleniumglutathione peroxidase
    • Rocher C, Lalanne JL, and Chaudière J. Purification and properties of a recombinant sulfur analog of murine seleniumglutathione peroxidase. Eur J Biochem 205: 955-960, 1992.
    • (1992) Eur J Biochem , vol.205 , pp. 955-960
    • Rocher, C.1    Lalanne, J.L.2    Chaudière, J.3
  • 69
    • 84875754602 scopus 로고    scopus 로고
    • Chemical basis for the use of selenocysteine
    • 3rd ed., edited by Hatfield DL, Berry MJ, and Gladyshev VN. New York: Springer
    • Ruggles EL, Snider GW, and Hondal RJ. Chemical basis for the use of selenocysteine. In: Selenium: ItsMolecular Biology and Role in Human Health. 3rd ed., edited by Hatfield DL, Berry MJ, and Gladyshev VN. New York: Springer, 2012, pp. 73-83.
    • (2012) Selenium: ItsMolecular Biology and Role in Human Health , pp. 73-83
    • Ruggles, E.L.1    Snider, G.W.2    Hondal, R.J.3
  • 71
    • 35348926287 scopus 로고    scopus 로고
    • Influence of pH and flanking serine on the redox potential of S-S and S-Se bridges of Cys-Cys and Cys-Sec peptides
    • Schneider A, Brandt W, and Wessjohann LA. Influence of pH and flanking serine on the redox potential of S-S and S-Se bridges of Cys-Cys and Cys-Sec peptides. Biol Chem 388: 1099-10101, 2007.
    • (2007) Biol Chem , vol.388 , pp. 1099-10101
    • Schneider, A.1    Brandt, W.2    Wessjohann, L.A.3
  • 73
    • 0028845121 scopus 로고
    • Catalysis of reduction of disulfide by selenol
    • Singh R and Kats L. Catalysis of reduction of disulfide by selenol. Anal Biochem 232: 86-91, 1995.
    • (1995) Anal Biochem , vol.232 , pp. 86-91
    • Singh, R.1    Kats, L.2
  • 74
    • 0025231755 scopus 로고
    • 1H NMR line shape analysis
    • Singh R and Whitesides GM. Comparison of rate constants for thiolate-disulfide interchange in water and polar aprotic solvents using dynamic 1H NMR line shape analysis. J Am Chem Soc 112: 1190-1197, 1990. (Pubitemid 20127072)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.3 , pp. 1190-1197
    • Singh, R.1    Whitesides, G.M.2
  • 75
    • 0000928578 scopus 로고
    • Degenerate intermolecular thiolate-disulfide interchange involving cyclic five-membered disulfides is faster by *103 than that involving six-or sevenmembered disulfides
    • Singh R and Whitesides GM. Degenerate intermolecular thiolate-disulfide interchange involving cyclic five-membered disulfides is faster by *103 than that involving six-or sevenmembered disulfides. J Am Chem Soc 112: 6304-6309, 1990.
    • (1990) J Am Chem Soc , vol.112 , pp. 6304-6309
    • Singh, R.1    Whitesides, G.M.2
  • 76
    • 78650865387 scopus 로고    scopus 로고
    • Methaneseleninic acid is a substrate for truncated thioredoxin reductase: Implications for the catalytic mechanism and redox signaling
    • Snider G, Grout L, Ruggles EL, and Hondal RJ. Methaneseleninic acid is a substrate for truncated thioredoxin reductase: implications for the catalytic mechanism and redox signaling. Biochemistry 49: 10329-10338, 2010.
    • (2010) Biochemistry , vol.49 , pp. 10329-10338
    • Snider, G.1    Grout, L.2    Ruggles, E.L.3    Hondal, R.J.4
  • 77
    • 79960870552 scopus 로고    scopus 로고
    • The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: Benzyl viologen oxidoreductase activity
    • Soboh B, Pinske C, Kuhns M, Waclawek M, Ihling C, Trchounian K, Trchounian A, Sinz A, and Sawers G. The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: benzyl viologen oxidoreductase activity. BMC Microbiol 11: 173, 2011.
    • (2011) BMC Microbiol , vol.11 , pp. 173
    • Soboh, B.1    Pinske, C.2    Kuhns, M.3    Waclawek, M.4    Ihling, C.5    Trchounian, K.6    Trchounian, A.7    Sinz, A.8    Sawers, G.9
  • 79
    • 77957132219 scopus 로고    scopus 로고
    • Selenium and sulfur in exchange reactions: A comparative study
    • Steinmann D, Nauser T, and Koppenol WH. Selenium and sulfur in exchange reactions: a comparative study. J Org Chem 75: 6696-6699, 2010.
    • (2010) J Org Chem , vol.75 , pp. 6696-6699
    • Steinmann, D.1    Nauser, T.2    Koppenol, W.H.3
  • 80
    • 33947466844 scopus 로고
    • Solvolytic displacement reactions at saturated carbon atoms
    • Streitwieser A. Jr. Solvolytic displacement reactions at saturated carbon atoms. Chem Rev 56: 571-752, 1956.
    • (1956) Chem Rev , vol.56 , pp. 571-752
    • Streitwieser Jr., A.1
  • 81
    • 81855209007 scopus 로고    scopus 로고
    • Catalytic activity of selenomethionine in removing amino acid, peptide, and protein hydroperoxides
    • Suryo RA and Davies MJ. Catalytic activity of selenomethionine in removing amino acid, peptide, and protein hydroperoxides. Free Radic Biol Med 51: 2289-2299, 2011.
    • (2011) Free Radic Biol Med , vol.51 , pp. 2289-2299
    • Suryo, R.A.1    Davies, M.J.2
  • 82
  • 83
    • 49749163427 scopus 로고
    • Enzymic deiodination of L-thyroxine and 3,5,3¢-triiodothyronine; Intracellular localization of deiodinase in rat brain and skeletal muscle
    • Tata Jr. Enzymic deiodination of L-thyroxine and 3,5,3¢- triiodothyronine; intracellular localization of deiodinase in rat brain and skeletal muscle. Biochim Biophys Acta 28: 801-811, 1958.
    • (1958) Biochim Biophys Acta , vol.28 , pp. 801-811
    • Tata, J.R.1
  • 84
    • 72649102227 scopus 로고    scopus 로고
    • Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme
    • Toppo S, Flohe L, Ursini F, Vanin S, and Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim Biophys Acta 1790: 1486-1500, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1486-1500
    • Toppo, S.1    Flohe, L.2    Ursini, F.3    Vanin, S.4    Maiorino, M.5
  • 87
    • 35348902569 scopus 로고    scopus 로고
    • Selenium in chemistry and biochemistry in comparison to sulfur
    • DOI 10.1515/BC.2007.138
    • Wessjohann LA, Schneider A, Abbas M, and Brandt W. Selenium in chemistry and biochemistry in comparison to sulfur. Biol Chem 388: 997-1006, 2007. (Pubitemid 47584312)
    • (2007) Biological Chemistry , vol.388 , Issue.10 , pp. 997-1006
    • Wessjohann, L.A.1    Schneider, A.2    Abbas, M.3    Brandt, W.4
  • 88
    • 84887317971 scopus 로고
    • Identification and synthesis of a naturally occurring selenonucleoside in bacterial tRNAs: 5-[(methylamino)methyl]-2-selenouridine
    • Wittwer AJ, Tsai L, Ching WM, and Stadtman TC. Identification and synthesis of a naturally occurring selenonucleoside in bacterial tRNAs: 5-[(methylamino)methyl]-2-selenouridine Proc Natl Acad Sci U S A 81: 57-60, 1984.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 57-60
    • Wittwer, A.J.1    Tsai, L.2    Ching, W.M.3    Stadtman, T.C.4
  • 90
    • 20444401524 scopus 로고    scopus 로고
    • Catalysis of thiol/disulfide exchange: Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities
    • DOI 10.1074/jbc.M411476200
    • Xiao R, Lundstrom-Ljung J, Holmgren A, and Gilbert HF. Catalysis of thiol/disulfide exchange: glutaredoxin 1 and protein disulfide isomerase use different mechanisms to enhance oxidase and reductase activities. J Biol Chem280: 21099-21106, 2005. (Pubitemid 40805669)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21099-21106
    • Xiao, R.1    Lundstrom-Ljung, J.2    Holmgren, A.3    Gilbert, H.F.4
  • 91
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • DOI 10.1074/jbc.M000690200
    • Zhong L and Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J Biol Chem 275: 18121-18128, 2000. (Pubitemid 30414762)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.