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Volumn 52, Issue 46, 2013, Pages 8323-8332

Human augmenter of liver regeneration: Probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase

Author keywords

[No Author keywords available]

Indexed keywords

APPARENT RATE CONSTANT; CATALYTIC MECHANISMS; CHARGE TRANSFER COMPLEX; CHARGE TRANSFER INTERACTION; FLAVIN CHROMOPHORES; NUCLEOPHILIC ATTACK; STERIC REQUIREMENTS; THIOL-DISULFIDE EXCHANGE REACTION;

EID: 84888256339     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401305w     Document Type: Article
Times cited : (14)

References (74)
  • 1
    • 0016769993 scopus 로고
    • Preparation and partial characterization of hepatic regenerative stimulator substance (SS) from rat liver
    • LaBrecque, D. R. and Pesch, L. A. (1975) Preparation and partial characterization of hepatic regenerative stimulator substance (SS) from rat liver J. Physiol. 248, 273-284
    • (1975) J. Physiol. , vol.248 , pp. 273-284
    • Labrecque, D.R.1    Pesch, L.A.2
  • 2
    • 0028122426 scopus 로고
    • Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: Expression of biologically active recombinant ALR and demonstration of tissue distribution
    • Hagiya, M., Francavilla, A., Polimeno, L., Ihara, I., Sakai, H., Seki, T., Shimonishi, M., Porter, K. A., and Starzl, T. E. (1994) Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distribution Proc. Natl. Acad. Sci. U.S.A. 91, 8142-8146
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8142-8146
    • Hagiya, M.1    Francavilla, A.2    Polimeno, L.3    Ihara, I.4    Sakai, H.5    Seki, T.6    Shimonishi, M.7    Porter, K.A.8    Starzl, T.E.9
  • 3
    • 0033527552 scopus 로고    scopus 로고
    • Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases
    • Hoober, K. L., Glynn, N. M., Burnside, J., Coppock, D. L., and Thorpe, C. (1999) Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases J. Biol. Chem. 274, 31759-31762
    • (1999) J. Biol. Chem. , vol.274 , pp. 31759-31762
    • Hoober, K.L.1    Glynn, N.M.2    Burnside, J.3    Coppock, D.L.4    Thorpe, C.5
  • 4
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee, J., Hofhaus, G., and Lisowsky, T. (2000) Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase FEBS Lett. 477 (1-2) 62-66
    • (2000) FEBS Lett. , vol.477 , Issue.12 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 5
    • 0035076003 scopus 로고    scopus 로고
    • Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase
    • Lisowsky, T., Lee, J. E., Polimeno, L., Francavilla, A., and Hofhaus, G. (2001) Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase Dig. Liver Dis. 33, 173-180
    • (2001) Dig. Liver Dis. , vol.33 , pp. 173-180
    • Lisowsky, T.1    Lee, J.E.2    Polimeno, L.3    Francavilla, A.4    Hofhaus, G.5
  • 7
    • 0034535032 scopus 로고    scopus 로고
    • Stimulation of the mitogen-activated protein kinase cascade and tyrosine phosphorylation of the epidermal growth factor receptor by hepatopoietin
    • Li, Y., Li, M., Xing, G., Hu, Z., Wang, Q., Dong, C., Wei, H., Fan, G., Chen, J., Yang, X., Zhao, S., Chen, H., Guan, K., Wu, C., Zhang, C., and He, F. (2000) Stimulation of the mitogen-activated protein kinase cascade and tyrosine phosphorylation of the epidermal growth factor receptor by hepatopoietin J. Biol. Chem. 275, 37443-37447
    • (2000) J. Biol. Chem. , vol.275 , pp. 37443-37447
    • Li, Y.1    Li, M.2    Xing, G.3    Hu, Z.4    Wang, Q.5    Dong, C.6    Wei, H.7    Fan, G.8    Chen, J.9    Yang, X.10    Zhao, S.11    Chen, H.12    Guan, K.13    Wu, C.14    Zhang, C.15    He, F.16
  • 8
    • 1542467584 scopus 로고    scopus 로고
    • The potentiation role of hepatopoietin on activator protein-1 is dependent on its sulfhydryl oxidase activity
    • Chen, X., Li, Y., Wei, K., Li, L., Liu, W., Zhu, Y., Qiu, Z., and He, F. (2003) The potentiation role of hepatopoietin on activator protein-1 is dependent on its sulfhydryl oxidase activity J. Biol. Chem. 278, 49022-49030
    • (2003) J. Biol. Chem. , vol.278 , pp. 49022-49030
    • Chen, X.1    Li, Y.2    Wei, K.3    Li, L.4    Liu, W.5    Zhu, Y.6    Qiu, Z.7    He, F.8
  • 9
    • 23844531544 scopus 로고    scopus 로고
    • Effect of naked eukaryotic expression plasmid encoding rat augmenter of liver regeneration on acute hepatic injury and hepatic failure in rats
    • Zhang, L. M., Liu, D. W., Liu, J. B., Zhang, X. L., Wang, X. B., Tang, L. M., and Wang, L. Q. (2005) Effect of naked eukaryotic expression plasmid encoding rat augmenter of liver regeneration on acute hepatic injury and hepatic failure in rats World J. Gastroenterol. 11, 3680-3685
    • (2005) World J. Gastroenterol. , vol.11 , pp. 3680-3685
    • Zhang, L.M.1    Liu, D.W.2    Liu, J.B.3    Zhang, X.L.4    Wang, X.B.5    Tang, L.M.6    Wang, L.Q.7
  • 10
    • 33748178465 scopus 로고    scopus 로고
    • ALR and Liver Regeneration
    • Pawlowski, R. and Jura, J. (2006) ALR and Liver Regeneration Mol. Cell. Biochem. 288, 159-169
    • (2006) Mol. Cell. Biochem. , vol.288 , pp. 159-169
    • Pawlowski, R.1    Jura, J.2
  • 11
    • 33748288398 scopus 로고    scopus 로고
    • Insights on augmenter of liver regeneration cloning and function
    • Gatzidou, E., Kouraklis, G., and Theocharis, S. (2006) Insights on augmenter of liver regeneration cloning and function World J. Gastroenterol. 12, 4951-4958
    • (2006) World J. Gastroenterol. , vol.12 , pp. 4951-4958
    • Gatzidou, E.1    Kouraklis, G.2    Theocharis, S.3
  • 15
    • 0037407929 scopus 로고    scopus 로고
    • The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase
    • Wu, C. K., Dailey, T. A., Dailey, H. A., Wang, B. C., and Rose, J. P. (2003) The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase Protein Sci. 12, 1109-1118
    • (2003) Protein Sci. , vol.12 , pp. 1109-1118
    • Wu, C.K.1    Dailey, T.A.2    Dailey, H.A.3    Wang, B.C.4    Rose, J.P.5
  • 16
    • 77955265541 scopus 로고    scopus 로고
    • Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy
    • Daithankar, V. N., Schaefer, S. A., Dong, M., Bahnson, B. J., and Thorpe, C. (2010) Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy Biochemistry 49, 6737-6745
    • (2010) Biochemistry , vol.49 , pp. 6737-6745
    • Daithankar, V.N.1    Schaefer, S.A.2    Dong, M.3    Bahnson, B.J.4    Thorpe, C.5
  • 18
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase-A family of flavoenzyme transhydrogenases
    • In (Müller, F. Ed.), pp, CRC Press, Chemistry and Biochemistry of Flavoenzymes
    • Williams, C. H., Jr. (1992) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase-A family of flavoenzyme transhydrogenases, In Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.), pp 121-211, CRC Press, Chemistry and Biochemistry of Flavoenzymes.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , pp. 121-211
    • Williams Jr., C.H.1
  • 19
    • 10644295071 scopus 로고    scopus 로고
    • Flavoprotein disulfide reductases: Advances in chemistry and function
    • Argyrou, A. and Blanchard, J. S. (2004) Flavoprotein disulfide reductases: advances in chemistry and function Prog. Nucleic Acid Res. Mol. Biol. 78, 89-142
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 89-142
    • Argyrou, A.1    Blanchard, J.S.2
  • 20
    • 84979150487 scopus 로고    scopus 로고
    • Flavoprotein disulfide reductases and structurally related flvoprotein thiol/disulfide-linked oxidoreductases
    • In (Hille, R. Miller, S. M. and Palfey, B. A. Eds.), pp, De Gruyter, Berlin
    • Miller, S. M. (2013) Flavoprotein disulfide reductases and structurally related flvoprotein thiol/disulfide-linked oxidoreductases, In Handbook of Flavoproteins (Hille, R., Miller, S. M., and Palfey, B. A., Eds.), pp 165-201, De Gruyter, Berlin.
    • (2013) Handbook of Flavoproteins , pp. 165-201
    • Miller, S.M.1
  • 21
    • 13444304104 scopus 로고    scopus 로고
    • Augmenter of liver regeneration: A flavin dependent sulfhydryl oxidase with cytochrome C reductase activity
    • Farrell, S. R. and Thorpe, C. (2005) Augmenter of liver regeneration: a flavin dependent sulfhydryl oxidase with cytochrome C reductase activity Biochemistry 44, 1532-1541
    • (2005) Biochemistry , vol.44 , pp. 1532-1541
    • Farrell, S.R.1    Thorpe, C.2
  • 22
    • 66649106947 scopus 로고    scopus 로고
    • Augmenter of liver regeneration: Substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space
    • Daithankar, V. N., Farrell, S. R., and Thorpe, C. (2009) Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space Biochemistry 48, 4828-4837
    • (2009) Biochemistry , vol.48 , pp. 4828-4837
    • Daithankar, V.N.1    Farrell, S.R.2    Thorpe, C.3
  • 24
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., and Herrmann, J. M. (2005) A disulfide relay system in the intermembrane space of mitochondria that mediates protein import Cell 121, 1059-1069
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 25
    • 79960454552 scopus 로고    scopus 로고
    • Gfer is a critical regulator of HSC proliferation
    • Sankar, U. and Means, A. R. (2011) Gfer is a critical regulator of HSC proliferation Cell Cycle 10, 2263-2268
    • (2011) Cell Cycle , vol.10 , pp. 2263-2268
    • Sankar, U.1    Means, A.R.2
  • 26
    • 77950630969 scopus 로고    scopus 로고
    • Growth Factor erv1-like Modulates Drp1 to Preserve Mitochondrial Dynamics and Function in Mouse Embryonic Stem Cells
    • Todd, L. R., Damin, M. N., Gomathinayagam, R., Horn, S. R., Means, A. R., and Sankar, U. (2010) Growth Factor erv1-like Modulates Drp1 to Preserve Mitochondrial Dynamics and Function in Mouse Embryonic Stem Cells Mol. Biol. Cell 21, 1226-1236
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1226-1236
    • Todd, L.R.1    Damin, M.N.2    Gomathinayagam, R.3    Horn, S.R.4    Means, A.R.5    Sankar, U.6
  • 27
    • 84888223684 scopus 로고    scopus 로고
    • Flavoproteins in oxidative protein folding
    • In (Hill, R. Miller, S. M. and Palfey, B. A. Eds.), pp, de Gruyter, Berlin
    • Thorpe, C. (2013) Flavoproteins in oxidative protein folding, In Handbook of Flavoproteins (Hill, R., Miller, S. M., and Palfey, B. A., Eds.), pp 248-269, de Gruyter, Berlin.
    • (2013) Handbook of Flavoproteins , pp. 248-269
    • Thorpe, C.1
  • 28
    • 41449101717 scopus 로고    scopus 로고
    • The Erv family of sulfhydryl oxidases
    • Fass, D. (2008) The Erv family of sulfhydryl oxidases Biochim. Biophys. Acta 1783, 557-566
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 557-566
    • Fass, D.1
  • 29
    • 84857591674 scopus 로고    scopus 로고
    • Erv2 and Quiescin Sulfhydryl Oxidases: Erv-Domain Enzymes Associated with the Secretory Pathway
    • Sevier, C. (2012) Erv2 and Quiescin Sulfhydryl Oxidases: Erv-Domain Enzymes Associated with the Secretory Pathway Antioxid. Redox Sign. 16, 800-808
    • (2012) Antioxid. Redox Sign. , vol.16 , pp. 800-808
    • Sevier, C.1
  • 30
    • 0000756406 scopus 로고
    • Equilibrium-Constants for Thiol Disulfide Interchange Reactions-a Coherent, Corrected Set
    • Lees, W. J. and Whitesides, G. M. (1993) Equilibrium-Constants for Thiol Disulfide Interchange Reactions-a Coherent, Corrected Set J. Org. Chem. 58, 642-647
    • (1993) J. Org. Chem. , vol.58 , pp. 642-647
    • Lees, W.J.1    Whitesides, G.M.2
  • 31
    • 0018405696 scopus 로고
    • Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis
    • Williams, C. H., Arscott, L. D., Matthews, R. G., Thorpe, C., and Wilkinson, K. D. (1980) Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis Methods Enzymol. 62D, 185-198
    • (1980) Methods Enzymol. , vol.62 , pp. 185-198
    • Williams, C.H.1    Arscott, L.D.2    Matthews, R.G.3    Thorpe, C.4    Wilkinson, K.D.5
  • 33
    • 60549112465 scopus 로고    scopus 로고
    • FitSpace explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) FitSpace explorer: an algorithm to evaluate multidimensional parameter space in fitting kinetic data Anal. Biochem. 387, 30-41
    • (2009) Anal. Biochem. , vol.387 , pp. 30-41
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 34
    • 60549105802 scopus 로고    scopus 로고
    • Global kinetic explorer: A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data Anal. Biochem. 387, 20-29
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 37
    • 0017067595 scopus 로고
    • Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase
    • Thorpe, C. and C. H. Williams, J. (1976) Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase J. Biol. Chem. 251, 3553-3557
    • (1976) J. Biol. Chem. , vol.251 , pp. 3553-3557
    • Thorpe, C.1    Williams J, C.H.2
  • 38
    • 42449098493 scopus 로고    scopus 로고
    • Human quiescin-sulfhydryl oxidase, QSOX1: Probing internal redox steps by mutagenesis
    • Heckler, E. J., Alon, A., Fass, D., and Thorpe, C. (2008) Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis Biochemistry 47, 4955-4963
    • (2008) Biochemistry , vol.47 , pp. 4955-4963
    • Heckler, E.J.1    Alon, A.2    Fass, D.3    Thorpe, C.4
  • 39
    • 0141765887 scopus 로고    scopus 로고
    • Avian sulfhydryl oxidase is not a metalloenzyme: Adventitious binding of divalent metal ions to the enzyme
    • Brohawn, S. G., Rudik, I., and Thorpe, C. (2003) Avian sulfhydryl oxidase is not a metalloenzyme: adventitious binding of divalent metal ions to the enzyme Biochemistry 42, 11074-11082
    • (2003) Biochemistry , vol.42 , pp. 11074-11082
    • Brohawn, S.G.1    Rudik, I.2    Thorpe, C.3
  • 40
    • 33947388374 scopus 로고    scopus 로고
    • Erv2p: Characterization of the redox behavior of a yeast sulfhydryl oxidase
    • Wang, W., Winther, J. R., and Thorpe, C. (2007) Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase Biochemistry 46, 3246-3254
    • (2007) Biochemistry , vol.46 , pp. 3246-3254
    • Wang, W.1    Winther, J.R.2    Thorpe, C.3
  • 41
    • 0001432326 scopus 로고
    • Enzymatic Synthesis of Deoxyribonucleotides.V. Purification and Properties of Thioredoxin Reductase from Escherichia coli B
    • Moore, E. C., Reichard, P., and Thelander, L. (1964) Enzymatic Synthesis of Deoxyribonucleotides.V. Purification and Properties of Thioredoxin Reductase from Escherichia coli B J. Biol. Chem. 239, 3445-3452
    • (1964) J. Biol. Chem. , vol.239 , pp. 3445-3452
    • Moore, E.C.1    Reichard, P.2    Thelander, L.3
  • 42
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause, G., Lundstrom, J., Barea, J. L., Pueyo de la Cuesta, C., and Holmgren, A. (1991) Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin J. Biol. Chem. 266, 9494-9500
    • (1991) J. Biol. Chem. , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3    Pueyo De La Cuesta, C.4    Holmgren, A.5
  • 43
    • 0039714219 scopus 로고    scopus 로고
    • Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases
    • Mossner, E., Huber-Wunderlich, M., and Glockshuber, R. (1998) Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases Protein Sci. 7, 1233-1244
    • (1998) Protein Sci. , vol.7 , pp. 1233-1244
    • Mossner, E.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 44
    • 0027254133 scopus 로고
    • The Reactive and Destabilizing Disulfide Bond of Dsba, a Protein Required for Protein Disulfide Bond Formation in Vivo
    • Zapun, A., Bardwell, J. C. A., and Creighton, T. E. (1993) The Reactive and Destabilizing Disulfide Bond of Dsba, a Protein Required for Protein Disulfide Bond Formation In Vivo Biochemistry 32, 5083-5092
    • (1993) Biochemistry , vol.32 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.A.2    Creighton, T.E.3
  • 45
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich, M. and Glockshuber, R. (1998) A single dipeptide sequence modulates the redox properties of a whole enzyme family Fold. Des. 3, 161-171
    • (1998) Fold. Des. , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 46
    • 0033564233 scopus 로고    scopus 로고
    • Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm
    • Jonda, S., Huber-Wunderlich, M., Glockshuber, R., and Mossner, E. (1999) Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm EMBO J. 18, 3271-3281
    • (1999) EMBO J. , vol.18 , pp. 3271-3281
    • Jonda, S.1    Huber-Wunderlich, M.2    Glockshuber, R.3    Mossner, E.4
  • 47
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Aslund, F., Berndt, K. D., and Holmgren, A. (1997) Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria J. Biol. Chem. 272, 30780-30786
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Aslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 48
    • 0037013828 scopus 로고    scopus 로고
    • Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade
    • Inaba, K. and Ito, K. (2002) Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade EMBO J. 21, 2646-2654
    • (2002) EMBO J. , vol.21 , pp. 2646-2654
    • Inaba, K.1    Ito, K.2
  • 50
    • 0037395242 scopus 로고    scopus 로고
    • The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
    • Hofhaus, G., Lee, J. E., Tews, I., Rosenberg, B., and Lisowsky, T. (2003) The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre Eur. J. Biochem. 270, 1528-1535
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1528-1535
    • Hofhaus, G.1    Lee, J.E.2    Tews, I.3    Rosenberg, B.4    Lisowsky, T.5
  • 51
    • 33646688670 scopus 로고    scopus 로고
    • Multidomain flavin-dependent sulfhydryl oxidases
    • Coppock, D. L. and Thorpe, C. (2006) Multidomain flavin-dependent sulfhydryl oxidases Antioxid. Redox Signal. 8, 300-311
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 300-311
    • Coppock, D.L.1    Thorpe, C.2
  • 52
    • 77749286237 scopus 로고    scopus 로고
    • Quiescin sulfhydryl oxidase from Trypanosoma brucei: Catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain
    • Kodali, V. K. and Thorpe, C. (2010) Quiescin sulfhydryl oxidase from Trypanosoma brucei: catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain Biochemistry 49, 2075-2085
    • (2010) Biochemistry , vol.49 , pp. 2075-2085
    • Kodali, V.K.1    Thorpe, C.2
  • 54
    • 0034712684 scopus 로고    scopus 로고
    • Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell
    • Arscott, L. D., Veine, D. M., and Williams, C. H., Jr. (2000) Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell Biochemistry 39, 4711-4721
    • (2000) Biochemistry , vol.39 , pp. 4711-4721
    • Arscott, L.D.1    Veine, D.M.2    Williams Jr., C.H.3
  • 55
    • 0017166209 scopus 로고
    • Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase
    • Thorpe, C. and Williams, C. H. (1976) Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase J. Biol. Chem. 251, 7726-7728
    • (1976) J. Biol. Chem. , vol.251 , pp. 7726-7728
    • Thorpe, C.1    Williams, C.H.2
  • 56
    • 0021342955 scopus 로고
    • Reconstitution of Escherichia coli thioredoxin reductase with 1-deazaFAD. Evidence for 1-deazaFAD C-4a adduct formation linked to the ionization of an active site base
    • O'Donnell, M. E. and Williams, C. H., Jr. (1984) Reconstitution of Escherichia coli thioredoxin reductase with 1-deazaFAD. Evidence for 1-deazaFAD C-4a adduct formation linked to the ionization of an active site base J. Biol. Chem. 259, 2243-2251
    • (1984) J. Biol. Chem. , vol.259 , pp. 2243-2251
    • O'Donnell, M.E.1    Williams Jr., C.H.2
  • 57
    • 0025363920 scopus 로고
    • Use of a site-directed triple mutant to trap intermediates: Demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase
    • Miller, S. M., Massey, V., Ballou, D., Williams, C. H., Jr., Distefano, M. D., Moore, M. J., and Walsh, C. T. (1990) Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase Biochemistry 29, 2831-2841
    • (1990) Biochemistry , vol.29 , pp. 2831-2841
    • Miller, S.M.1    Massey, V.2    Ballou, D.3    Williams Jr., C.H.4    Distefano, M.D.5    Moore, M.J.6    Walsh, C.T.7
  • 58
    • 84863044213 scopus 로고    scopus 로고
    • Flavin-linked Erv-family sulfhydryl oxidases release superoxide anion during catalytic turnover
    • Daithankar, V. N., Wang, W., Trujillo, J. R., and Thorpe, C. (2012) Flavin-linked Erv-family sulfhydryl oxidases release superoxide anion during catalytic turnover Biochemistry 51, 265-272
    • (2012) Biochemistry , vol.51 , pp. 265-272
    • Daithankar, V.N.1    Wang, W.2    Trujillo, J.R.3    Thorpe, C.4
  • 59
  • 60
    • 84978937530 scopus 로고    scopus 로고
    • The reactivity of oxygen with flavoproteins
    • In (Chapman, S. Perham, R. and Scrutton, N. S. Eds.), pp, Walter De Gruyter
    • Massey, V. (2002) The reactivity of oxygen with flavoproteins, In Flavins and Flavoproteins, International Congress Series (Chapman, S., Perham, R., and Scrutton, N. S., Eds.), pp 3-11, Walter De Gruyter.
    • (2002) Flavins and Flavoproteins, International Congress Series , pp. 3-11
    • Massey, V.1
  • 61
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes Trends Biochem. Sci. 31, 276-283
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 62
    • 0033537679 scopus 로고    scopus 로고
    • Egg white sulfhydryl oxidase: Kinetic mechanism of the catalysis of disulfide bond formation
    • Hoober, K. L. and Thorpe, C. (1999) Egg white sulfhydryl oxidase: Kinetic mechanism of the catalysis of disulfide bond formation Biochemistry 38, 3211-3217
    • (1999) Biochemistry , vol.38 , pp. 3211-3217
    • Hoober, K.L.1    Thorpe, C.2
  • 63
    • 30744436853 scopus 로고    scopus 로고
    • Determination of the distance between the two neutral flavin radicals in augmenter of liver regeneration by pulsed ELDOR
    • Kay, C. W. M., Elsasser, C., Bittl, R., Farrell, S. R., and Thorpe, C. (2006) Determination of the distance between the two neutral flavin radicals in augmenter of liver regeneration by pulsed ELDOR J. Am. Chem. Soc. 128, 76-77
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 76-77
    • Kay, C.W.M.1    Elsasser, C.2    Bittl, R.3    Farrell, S.R.4    Thorpe, C.5
  • 64
    • 0023066152 scopus 로고
    • Measurement of Thiol Disulfide Interchange Reactions and Thiol Pka Values
    • Houk, J., Singh, R., and Whitesides, G. M. (1987) Measurement of Thiol Disulfide Interchange Reactions and Thiol Pka Values Meth. Enzymol. 143, 129-140
    • (1987) Meth. Enzymol. , vol.143 , pp. 129-140
    • Houk, J.1    Singh, R.2    Whitesides, G.M.3
  • 65
    • 0026633682 scopus 로고
    • Lipoamide dehydrogenase from Azotobacter vinelandii: Site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes
    • Benen, J., van Berkel, W., Dieteren, N., Arscott, D., Williams, C., Jr., Veeger, C., and de Kok, A. (1992) Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes Eur. J. Biochem. 207, 487-497
    • (1992) Eur. J. Biochem. , vol.207 , pp. 487-497
    • Benen, J.1    Van Berkel, W.2    Dieteren, N.3    Arscott, D.4    Williams Jr., C.5    Veeger, C.6    De Kok, A.7
  • 66
    • 0000537410 scopus 로고
    • Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
    • Massey, V., Gibson, Q. H., and Veeger, C. (1960) Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase) Biochem. J. 77, 341-351
    • (1960) Biochem. J. , vol.77 , pp. 341-351
    • Massey, V.1    Gibson, Q.H.2    Veeger, C.3
  • 68
    • 33845283266 scopus 로고
    • Structure Reactivity Relations for Thiol Disulfide Interchange
    • Houk, J. and Whitesides, G. M. (1987) Structure Reactivity Relations for Thiol Disulfide Interchange J. Am. Chem. Soc. 109, 6825-6836
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6825-6836
    • Houk, J.1    Whitesides, G.M.2
  • 69
    • 84953396717 scopus 로고
    • Thiol-disulfide Interchange
    • In (Patai, S. and Rappoport, Z. Eds.), pp, John Wiley, New York
    • Singh, R. and Whitesides, G. (1993) Thiol-disulfide Interchange, In The Chemistry of Sulphur-Containing Functional Groups (Patai, S. and Rappoport, Z., Eds.), pp 633-658, John Wiley, New York.
    • (1993) The Chemistry of Sulphur-Containing Functional Groups , pp. 633-658
    • Singh, R.1    Whitesides, G.2
  • 70
    • 33847090263 scopus 로고
    • Directional Preferences of Nonbonded Atomic Contacts with Divalent Sulfur 0.1. Electrophiles and Nucleophiles
    • Rosenfield, R. E., Parthasarathy, R., and Dunitz, J. D. (1977) Directional Preferences of Nonbonded Atomic Contacts with Divalent Sulfur 0.1. Electrophiles and Nucleophiles J. Am. Chem. Soc. 99, 4860-4862
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 4860-4862
    • Rosenfield, R.E.1    Parthasarathy, R.2    Dunitz, J.D.3
  • 71
    • 0347719283 scopus 로고    scopus 로고
    • Theoretical insights into the mechanism for thiol/disulfide exchange
    • Fernandes, P. A. and Ramos, M. J. (2004) Theoretical insights into the mechanism for thiol/disulfide exchange Chemistry 10, 257-266
    • (2004) Chemistry , vol.10 , pp. 257-266
    • Fernandes, P.A.1    Ramos, M.J.2
  • 72
    • 37549062553 scopus 로고    scopus 로고
    • Mechanism of thiolate-disulfide interchange reactions in biochemistry
    • Bach, R. D., Dmitrenko, O., and Thorpe, C. (2008) Mechanism of thiolate-disulfide interchange reactions in biochemistry J. Org. Chem. 73, 12-21
    • (2008) J. Org. Chem. , vol.73 , pp. 12-21
    • Bach, R.D.1    Dmitrenko, O.2    Thorpe, C.3
  • 73


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