Flavoprotein disulfide reductases and structurally related flavoprotein thiol/disulfi de-linked oxidoreductases

Handbook of Flavoproteins: Complex Flavoproteins, Dehydrogenases and Physical Methods

Volumn 2, Issue , 2013, Pages 165-202

  Miller, Susan M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84979150487     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1515/9783110298345.165     Document Type: Chapter

References (94)

1. Argyrou A, Blanchard JS. Flavoprotein disulfide reductases: advances in chemistry and function. Prog Nucleic Acid Res Mol Biol 2004;78:89-142.
2. Williams CH, Jr. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase—a family of flavoenzyme transhydrogenases. In: Muller F, ed. Chemistry and Biochemistry of Flavoenzymes. Boca Raton: CRC Press; 1992:121-211.
3. Williams CH, Jr. Flavin-containing dehydrogenases. In: Boyer PD, ed. The Enzymes. New York: Academic Press; 1976:89-173.
4. Lennon BW, Williams CH, Jr., Ludwig ML. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science 2000;289:1190-4.
5. Massey V, Veeger C. Biological oxidations. Ann Rev Biochem 1963;32:579-638.
6. Schulz GE, Schirmer RH, Sachsenheimer W, Pai EF. The structure of the flavoenzyme glutathione reductase. Nature 1978;273:120-4.
7. 2 as the substrate. Biochemistry 1998;37:11496-507.
8. 2 as the substrate. Biochemistry 1999;38:853-4.
9. Sahlman L, Lambeir AM, Lindskog S. Rapid-scan stopped-flow studies of the pH dependence of the reaction between mercuric reductase and NADPH. Eur J of Biochem/FEBS 1986;156:479-88.
10. Thorpe C, Williams CH, Jr. Lipoamide dehydrogenase from pig heart. Pyridine nucleotide induced changes in monoalkylated two-electron reduced enzyme. Biochemistry 1981;20: 1507-13.
11. Miller SM, Massey V, Ballou D, Williams CH, Jr, Distefano MD, Moore MJ, Walsh CT. 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 1990;29:2831-41.
12. 2 into the active site of mercuric ion reductase depend on the nature of the X ligands. Biochemistry 1999;38:3519-29.
13. Thorpe C, Williams CH, Jr. Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase. J Biol Chem 1976;251:3553-7.
14. Reed LJ. Multienzyme complexes. Acc Chem Res 1974;7:40-6.
15. Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol 2005;350:543-52.
16. Brautigam CA, Wynn RM, Chuang JL, Machius M, Tomchick DR, Chuang DT. Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure 2006;14:611-21.
17. Brautigam CA, Wynn RM, Chuang JL, Naik MT, Young BB, Huang TH, Chuang DT. Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. J Biol Chem 2011;286:23476-88.
18. Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin- like protein. Science 2002;295:1073-7.
19. Rajashankar KR, Bryk R, Kniewel R, Buglino JA, Nathan CF, Lima CD. Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis. J Biol Chem 2005;280:33977-83.
20. Bryk R, Arango N, Venugopal A, Warren JD, Park YH, Patel MS, Lima CD, Nathan C. Triaza-spirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase. Biochemistry 2010;49:1616-27.
21. Cussiol JR, Alegria TG, Szweda LI, Netto LE. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. J Biol Chem 2010;285:21943-50.
22. Berkholz DS, Faber HR, Savvides SN, Karplus PA. Catalytic cycle of human glutathione reductase near 1 Ä resolution. J Mol Biol 2008;382:371-84.
23. Van Petegem F, De Vos D, Savvides S, Vergauwen B, Van Beeumen J. Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase. J Mol Biol 2007;374:883-9.
24. Bartsch RG, Newton GL, Sherrill C, Fahey RC. Glutathione amide and its perthiol in anaerobic sulfur bacteria. J Bacteriol 1996;178:4742-6.
25. Pott AS, Dahl C. Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosumare involved in the oxidation of intracellular sulfur. Microbiology 1998;144(Pt 7):1881-94.
26. Vergauwen B, Pauwels F, Jacquemotte F, Meyer TE, Cusanovich MA, Bartsch RG, Van Beeumen JJ. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J Biol Chem 2001;276:20890-7.
27. Scrutton NS, Berry A, Perham RN. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 1990;343:38-43.
28. Olin-Sandoval V, Moreno-Sanchez R, Saavedra E. Targeting trypanothione metabolism in trypanosomatid human parasites. Current drug targets 2010;11:1614-30.
29. Salmon-Chemin L, Buisine E, Yardley V, Kohler S, Debreu MA, Landry V, Sergheraert C, Croft SL, Krauth-Siegel RL, Davioud-Charvet E. 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity. J Med Chem 2001;44:548-65.
30. Buchholz K, Schirmer RH, Eubel JK, Akoachere MB, Dandekar T, Becker K, Gromer S. Interactions of methylene blue with human disulfide reductases and their orthologues from Plasmodium falciparum. Antimicrob Agents Chemother 2008;52:183-91.
31. Spies HS, Steenkamp DJ. Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis. Eur J Biochem/FEBS 1994;224:203-13.
32. Barkay T, Miller SM, Summers AO. Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev 2003;27:355-84.
33. Barkay T, Kritee K, Boyd E, Geesey G. A thermophilic bacterial origin and subsequent constraints by redox, light and salinity on the evolution of the microbial mercuric reductase. Environ Microbiol 2010;12:2904-17.
34. Hong B, Nauss R, Harwood IM, Miller SM. Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved gam-ma-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione. Biochemistry 2010;49:8187-96.
35. Johs A, Harwood IM, Parks JM, Nauss RE, Smith JC, Liang L, Miller SM. Structural characterization of intramolecular Hg(2+) transfer between flexibly linked domains of mercuric ion reductase. J Mol Biol 2011;413:639-56.
36. Ledwidge R, Hong B, Dotsch V, Miller SM. NmerA of Tn507 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols. Biochemistry 2010;49:8988-98.
37. 2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. Biochemistry 2005;44:11402-16.
38. Ledwidge R, Soinski R, Miller SM. Direct monitoring of metal ion transfer between two trafficking proteins. J Am Chem Soc 2005;127:10842-3.
39. Schiering N, Kabsch W, Moore MJ, Distefano MD, Walsh CT, Pai EF. Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607. Nature 1991;352:168-72.
40. Holmgren A, Lu J. Thioredoxin and thioredoxin reductase: current research with special reference to human disease. Biochem Biophys Res Commun 2010;396:120-4.
41. Hatfield DL, Gladyshev VN. How selenium has altered our understanding of the genetic code. Mol Cell Biol 2002;22:3565-76.
42. Arner ES. Focus on mammalian thioredoxin reductases—important selenoproteins with versatile functions. Biochim Biophys Acta 2009;1790:495-526.
43. Biterova EI, Turanov AA, Gladyshev VN, Barycki JJ. Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism. Proc Natl Acad Sci USA 2005;102:15018-23.
44. Fritz-Wolf K, Kehr S, Stumpf M, Rahlfs S, Becker K. Crystal structure of the human thioredoxin reductase-thioredoxin complex. Nat Commun 2011;2:383.
45. Fritz-Wolf K, Urig S, Becker K. The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis. J Mol Biol 2007;370:116-27.
46. Cheng Q, Sandalova T, Lindqvist Y, Arner ES. Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1. J Biol Chem 2009;284:3998-4008.
47. Angelucci F, Dimastrogiovanni D, Boumis G, Brunori M, Miele AE, Saccoccia F, Bellelli A. Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallography. J Biol Chem 2010;285:32557-67.
48. Angelucci F, Miele AE, Boumis G, Dimastrogiovanni D, Brunori M, Bellelli A. Glutathione reductase and thioredoxin reductase at the crossroad: the structure of Schistosoma mansoni thioredoxin glutathione reductase. Proteins 2008;72:936-45.
49. Kuriyan J, Krishna TS, Wong L, Guenther B, Pahler A, Williams CH, Jr, Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991;352:172-4.
50. Waksman G, Krishna TS, Williams CH, Jr., Kuriyan J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J Mol Biol 1994;236:800-16.
51. Lennon BW, Williams CH, Jr., Ludwig ML. Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor. Prot Sci 1999;8:2366-79.
52. Williams CH, Arscott LD, Muller S, Lennon BW, Ludwig ML, Wang PF, Veine DM, Becker K, Schirmer RH. Thioredoxin reductase two modes of catalysis have evolved. Eur J Biochem/FEBS 2000;267:6110-7.
53. Prongay AJ, Williams CH, Jr. Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs. J Biol Chem 1990;265:18968-75.
54. Negri A, Rodriguez-Larrea D, Marco E, Jimenez-Ruiz A, Sanchez-Ruiz JM, Gago F. Proteinprotein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase. Proteins 2010;78:36-51.
55. Hamill MJ, Chobot SE, Hernandez HH, Drennan CL, Elliott SJ. Direct electrochemical analyses of a thermophilic thioredoxin reductase: interplay between conformational change and redox chemistry. Biochemistry 2008;47:9738-46.
56. Jonsson TJ, Ellis HR, Poole LB. Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system. Biochemistry 2007;46:5709-21.
57. Helmann JD. Bacillithiol, a new player in bacterial redox homeostasis. Antioxidants & redox signaling 2011;15:123-33.
58. Cheng YQ, Yang M, Matter AM. Characterization of a gene cluster responsible for the biosynthesis of anticancer agent FK228 in Chromobacterium violaceum No. 968. Appl Environ Microb 2007;73:3460-9.
59. Li B, Forseth RR, Bowers AA, Schroeder FC, Walsh CT. A backup plan for self-protection: S-methylation of holomycin biosynthetic intermediates in Streptomyces clavuligerus. ChemBioChem 2012;13:2521-6.
60. Li B, Walsh CT. Streptomyces clavuligerus HlmI is an intramolecular disulfide-forming dithiol oxidase in holomycin biosynthesis. Biochemistry 2011;50:4615-22.
61. Scharf DH, Heinekamp T, Remme N, Hortschansky P, Brakhage AA, Hertweck C. Biosynthesis and function of gliotoxin in Aspergillus fumigatus. Appl Microbiol Biot 2012;93:467-72.
62. Scharf DH, Remme N, Heinekamp T, Hortschansky P, Brakhage AA, Hertweck C. Transan-nular disulfide formation in gliotoxin biosynthesis and its role in self-resistance of the human pathogen Aspergillus fumigatus. J Am Chem Soc 2010;132:10136-41.
63. Wang C, Wesener SR, Zhang H, Cheng YQ. An FAD-dependent pyridine nucleotide-disulfide oxidoreductase is involved in disulfide bond formation in FK228 anticancer depsipeptide. Chem Biol 2009;16:585-93.
64. Claiborne A, Mallett TC, Yeh JI, Luba J, Parsonage D. Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation. Adv Protein Chem 2001;58:215-76.
65. 2 into two water molecules by the flavoenzyme. Biochemistry 2006;45:9648-59.
66. delCardayre SB, Stock KP, Newton GL, Fahey RC, Davies JE. Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J Biol Chem 1998;273:5744-51.
67. Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A. Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution. Biochemistry 2006;45:11278-89.
68. Wallen JR, Mallett TC, Boles W, Parsonage D, Furdui CM, Karplus PA, Claiborne A. Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking. Biochemistry 2009;48:9650-67.
69. Mueller EG. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2006;2:185-94.
70. Ensign SA. Microbial metabolism of aliphatic alkenes. Biochemistry 2001;40:5845-53.
71. Krum JG, Ensign SA. Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis in Xanthobacter strain Py2. J Bacteriol 2001;183:2172-7.
72. Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW. Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Acta Crystal-logr D 2001;57:445-7.
73. 2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Biochemistry 2002;41:12907-13.
74. Pandey AS, Mulder DW, Ensign SA, Peters JW. Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase. FEBS Lett 2011;585:459-64.
75. Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW. Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Biochemistry 2006;45:113-20.
76. Clark DD, Allen JR, Ensign SA. Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system. Biochemistry 2000;39:1294-304.
77. Kofoed MA, Wampler DA, Pandey AS, Peters JW, Ensign SA. Roles of the redox-active disulfide and histidine residues forming a catalytic dyad in reactions catalyzed by 2-ketopropyl coenzyme M oxidoreductase/carboxylase. J Bacteriol 2011;193:4904-13.
78. Boyd JM, Clark DD, Kofoed MA, Ensign SA. Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate. J Biol Chem 2010;285:25232-42.
79. Krishnakumar AM, Sliwa D, Endrizzi JA, Boyd ES, Ensign SA, Peters JW. Getting a handle on the role of coenzyme M in alkene metabolism. Microbiol Mol Biol Rev 2008;72: 445-56.
80. Warlick BP, Evans BS, Erb TJ, Ramagopal UA, Sriram J, Imker HJ, Sauder JM, Bonanno JB, Burley SK, Tabita FR, Almo SC, Sweedler JS, Gerlt JA. 1-methylthio-D-xylulose 5-phosphate methylsulfurylase: a novel route to 1-deoxy-D-xylulose 5-phosphate in Rhodospirillum rubrum. Biochemistry 2012;51:8324-6.
81. Marcia M, Ermler U, Peng G, Michel H. A new structure-based classification of sulfide:quinone oxidoreductases. Proteins 2010;78:1073-83.
82. 2S be the third endogenous gaseous transmitter? FASEB J 2002;16:1792-8.
83. Marcia M, Ermler U, Peng G, Michel H. The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 2009;106:9625-30.
84. Cherney MM, Zhang Y, James MN, Weiner JH. Structure-activity characterization of sulfide:quinone oxidoreductase variants. J Struct Biol 2012;178:319-28.
85. Cherney MM, Zhang Y, Solomonson M, Weiner JH, James MN. Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfido-trophic respiration and detoxification. J Mol Biol 2010;398:292-305.
86. Brito JA, Sousa FL, Stelter M, Bandeiras TM, Vonrhein C, Teixeira M, Pereira MM, Archer M. Structural and functional insights into sulfide:quinone oxidoreductase. Biochemistry 2009;48:5613-22.
87. Yeh JI, Claiborne A, Hol WG. Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 Ä resolution. Biochemistry 1996;35:9951-7.
88. The PyMOL Molecular Graphics System, version 1.4.1 Schrödinger, LLC.
89. Patterson S, Alphey MS, Jones DC, Shanks EJ, Street IP, Frearson JA, Wyatt PG, Gilbert IH, Fairlamb AH. Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: discovery, synthesis, and characterization of their binding mode by protein crystallography. J Med Chem 2011;54:6514-30.
90. Fox BS, Walsh CT. Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide. Biochemistry 1983;22:4082-8.
91. Sahlman L, Lambeir AM, Lindskog S, Dunford HB. The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa. J Biol Chem 1984;259:12403-8.
92. Miller SM, Moore MJ, Massey V, Williams CH, Jr, Distefano MD, Ballou DP, Walsh CT. Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry 1989;28:1194-205.
93. Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 2005;44:10583-92.
94. Wood ZA, Poole LB, Karplus PA. Structure of intact AhpF reveals a mirrored thioredox i n-like active site and implies large domain rotations during catalysis. Biochemistry 2001;40: 3900-11.