Structural studies of glutathione reductase family

Last modified: Thu Apr 15 13:41:56 BST 2004

• Aboagye-Kwarteng, T., Smith, K. and Fairlamb, A.H. (1992) Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism. Mol. Microbiol. 6, 3089-3099.
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• Bond, C.S., Zhang, Y., Berriman, M., Cunningham, M.L., Fairlamb, A.H. and Hunter, W.N. (1999) Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors. Structure 7, 81-89.
• Bradley, M., Bucheler, U.S. and Walsh, C.T. (1991) Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase. Biochemistry 30, 6124-6127.
• Carothers, D.J., Pons, G. and Patel, M.S. (1989) Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 268, 409-425.
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• Claiborne, A., Miller, H., Parsonage, D. and Ross, R.P. (1993) Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J. 7, 1483-1490.
• Crane, E.J., III, Vervoort, J. and Claiborne, A. (1997) ¹³C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase. Biochemistry 36, 8611-8618.
• Crane, E.J., III, Yeh, J.I., Luba, J. and Claiborne, A. (2000) Analysis of the kinetic and redox properties of the NADH peroxidase R303M mutant: Correlation with the crystal structure. Biochemistry 39, 10353-10364.
• Cunningham, M.L., Zvelebil, M.J. and Fairlamb, A.H. (1994) Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals. Eur. J. Biochem. 221, 285-295.
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• de Kok, A. and Visser, A.J. (1987) Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time-resolved flavin fluorescence. FEBS Lett. 218, 135-138.
• de la Sierra, I.L., Pernot, L., Prangé, T., Saludjian, P., Schiltz, M., Fourme, R. and Padrón, G. (1997) Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis. J. Mol. Biol. 269, 129-141.
• Ermler, U. and Schulz, G.E. (1991) The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 Å resolution. Proteins 9, 174-179.
• Ermler, U., Ghisla, S., Massey, V. and Schulz, G.E. (1991) Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues. Eur. J. Biochem. 199, 133-138.
• Henderson, G.B., Murgolo, N.J., Kuriyan, J., Osapay, K., Kominos, D., Berry, A., Scrutton, N.S., Hinchliffe, N.W., Perham, R.N. and Cerami, A. (1991) Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction. Proc. Natl. Acad. Sci. USA 88, 8769-8773.
• Hunter, W.H., Bailey, S., Habash, J., Harrop, S.J., Helliwell, J.R., Aboagye-Kwarteng, T., Smith, K. and Fairlamb, A.H. (1992) Active site of trypanothione reductase. A target for rational drug design. J. Mol. Biol. 227, 322-333.
• Jacoby, E.M., Schlichting, I., Lantwin, C.B., Kabsch, W. and Krauth-Siegel, R.L. (1996) Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex. Proteins 24, 73-80.
• Janes, W. and Schulz, G.E. (1990a) Role of the charged groups of glutathione disulfide in the catalysis of glutathione reductase: crystallographic and kinetic studies with synthetic analogues. Biochemistry 29, 4022-4030.
• Janes, W. and Schulz, G.E. (1990b) The binding of the retro-analogue of glutathione disulfide to glutathione reductase. J. Biol. Chem. 265, 10443-10445.
• Jentoft, J.E., Shoham, M., Hurst, D. and Patel, M.S. (1992) A structural model for human dihydrolipoamide dehydrogenase. Proteins 14, 88-101.
• Karplus, P.A. and Schulz, G.E. (1987) Refined structure of glutathione reductase at 1.54 Å resolution. J. Mol. Biol. 195, 701-729.
• Karplus, P.A. and Schulz, G.E. (1989) Substrate binding and catalysis by glutathione reductase as derived from refined enzyme:substrate crystal structures at 2 Å resolution. J. Mol. Biol. 210, 163-180.
• Karplus, P.A., Krauth-Siegel, R.L., Schirmer, R.H. and Schulz, G.E. (1988) Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis. Eur. J. Biochem. 171, 193-198.
• Karplus, P.A., Pai, E.F. and Schulz, G.E. (1989) A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution. Eur. J. Biochem. 178, 693-703.
• Krauth-Siegel, R.L., Schirmer, R.H. and Ghisla, S. (1985) FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure. Eur. J. Biochem. 148, 335-344.
• Kuriyan, J., Kong, X.-P., Krishna, T.S.R., Sweet, R.M., Murgolo, N.J., Field, H., Cerami, A. and Henderson, G.B. (1991a) X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-Å resolution. Proc. Natl. Acad. Sci. USA 88, 8764-8768.
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• Lantwin, C.B., Schlichting, I., Kabsch, W., Pai, E.F. and Krauth-Siegel, R.L. (1994) The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state. Proteins 18, 161-173.
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• Le Questel, J.Y., Morris, D.G., Maccallum, P.H., Poet, R. and Milner-White, E.J. (1993) Common ring motifs in proteins involving asparagine or glutamine amide groups hydrogen-bonded to main-chain atoms. J. Mol. Biol. 231, 888-896.
• Lim, L.W., Shamala, N., Mathews, F.S., Steenkamp, D.J., Hamlin, R. and Xuong, N.H. (1986) Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-Å resolution. J. Biol. Chem. 261, 15140-15146.
• Maeda-Yorita, K., Russell, G.C., Guest, J.R., Massey, V. and Williams, C.H., Jr. (1991) Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain. Biochemistry 30, 11788-11795.
• Mande, S.S., Sarfaty, S., Allen, M.D., Perham, R.N. and Hol, W.G.J. (1996) Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: Dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Structure 4, 277-286.
• Mattevi, A., Schierbeek, A.J. and Hol, W.G.J. (1991) Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution. A comparison with the structure of glutathione reductase. J. Mol. Biol. 220, 975-994.
• Mattevi, A., Obmolova, G., Sokatch, J.R., Betzel, C. and Hol, W.G.J. (1992) The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD⁺ at 2.45 Å resolution. Proteins 13, 336-351.
• Mattevi, A., Obmolova, G., Kalk, K.H., van Berkel, W.J. and Hol, W.G.J. (1993) Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 Å resolution. Analysis of redox and thermostability properties. J. Mol. Biol. 230, 1200-1215.
• Miller, H., Mande, S.S., Parsonage, D., Sarfaty, S.H., Hol, W.G.J. and Claiborne, A. (1995) An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide. Biochemistry 34, 5180-5190.
• Mittl, P.R.E. and Schulz, G.E. (1994) Structure of glutathione reductase from Escherichia coli at 1.86 Å resolution: comparison with the enzyme from human erythrocytes. Protein Science 3, 799-809.
• Mittl, P.R.E., Berry, A., Scrutton, N.S., Perham, R.N. and Schulz, G.E. (1993) Structural differences between wild-type NADP-dependent glutathione reductase from Escherichia coli and a redesigned NAD-dependent mutant. J. Mol. Biol. 231, 191-195.
• Mittl, P.R.E., Berry, A., Scrutton, N.S., Perham, R.N. and Schulz, G.E. (1994) Anatomy of an engineered NAD-binding site. Protein Science 3, 1504-1514.
• Mulrooney, S.B. and Williams, C.H., Jr. (1994) Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis. Biochemistry 33, 3148-3154.
• Pai, E.F. and Schulz, G.E. (1983) The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. J. Biol. Chem. 258, 1752-1757.
• Pai, E.F., Karplus, P.A. and Schulz, G.E. (1988) Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase. Biochemistry 27, 4465-4474.
• Parsonage, D. and Claiborne, A. (1995) Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center. Biochemistry 34, 435-441.
• Perham, R.N., Scrutton, N.S. and Berry, A. (1991) New enzymes for old: redesigning the coenzyme and substrate specificities of glutathione reductase. Bioessays 13, 515-525.
• Petsko, G.A. (1991) Déjà vu all over again. Nature 352, 104-105.
• Rennex, D., Cummings, R.T., Pickett, M., Walsh, C.T. and Bradley, M. (1994) Role of tyrosine residues in Hg(II) detoxification by mercuric reductase from Bacillus sp. strain RC607. Biochemistry 32, 7475-7478.
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• Rescigno, M. and Perham, R.N. (1994) Structure of the NADPH-binding motif of glutathione reductase: efficiency determined by evolution. Biochemistry 33, 5721-5727.
• Savvides, S.N. and Karplus, P.A. (1996) Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J. Biol. Chem. 271, 8101-8107.
• Schierbeek, A.J., Swarte, M.B., Dijkstra, B.W., Vriend, G., Read, R.J., Hol, W.G.J., Drenth, J. and Betzel, C. (1989) X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. J. Mol. Biol. 206, 365-379.
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• Schulz, G.E. (1980) Gene duplication in glutathione reductase. J. Mol. Biol. 138, 335-347.
• Schulz, G.E. and Karplus, P.A. (1988) High resolution structure and catalytic action of human glutathione reductase. Biochem. Soc. Trans. 16, 81-84.
• Schulz, G.E., Schirmer, R.H., Sachsenheimer, W. and Pai, E.F. (1978) The structure of the flavoenzyme glutathione reductase. Nature 273, 120-124.
• Schulz, G.E., Schirmer, R.H. and Pai, E.F. (1982) FAD-binding site of glutathione reductase. J. Mol. Biol. 160, 287-308.
• Stehle, T., Ahmed, S.A., Claiborne, A. and Schulz, G.E. (1990) The structure of NADH peroxidase from Streptococcus faecalis at 3.3 Å resolution. FEBS Lett. 267, 186-188.
• Stehle, T., Ahmed, S.A., Claiborne, A. and Schulz, G.E. (1991) Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 Å resolution. J. Mol. Biol. 221, 1325-1344.
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