| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
The FASEB Journal, Vol 9, 1267-1276, Copyright © 1995 by The Federation of American Societies for Experimental Biology
REVIEWS |
CH Williams Jr
Department of Veterans Affairs Medical Center, Department of Biological Chemistry, University of Michigan, Ann Arbor 48105, USA.
The flavoprotein thioredoxin reductase catalyzes the reduction of the small redox protein thioredoxin by NADPH. Thioredoxin reductase contains a redox active disulfide and is a member of the pyridine nucleotide-disulfide oxidoreductase family of flavoenzymes that includes lipoamide dehydrogenase, glutathione reductase, trypanothione reductase, mercuric reductase, and NADH peroxidase. The structure of thioredoxin reductase has recently been determined from X-ray crystallographic data. In this paper, we attempt to correlate the structure with a considerable body of mechanistic data and to arrive at a mechanism consistent with both. The path of reducing equivalents in catalysis by glutathione reductase and lipoamide dehydrogenase is clear. To envisage the path of reducing equivalents in catalysis by thioredoxin reductase, a conformational change is required in which the NADPH domain rotates relative to the FAD domain. The rotation moves the nascent dithiol from its observed position adjacent to the re surface of the flavin ring system toward the protein surface for dithiol- disulfide interchange with the protein substrate thioredoxin and moves the nicotinamide ring of NADPH adjacent to the flavin ring for efficient hydride transfer. Reverse rotation allows reduction of the redox active disulfide by the reduced flavin. This requires that the enzyme pass through a ternary complex; the kinetic evidence for such a complex is discussed.
This article has been cited by other articles:
|
|
 |
|
  G. Hagelueken, L. Wiehlmann, T. M. Adams, H. Kolmar, D. W. Heinz, B. Tummler, and W.-D. Schubert Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa PNAS, July 24, 2007; 104(30): 12276 - 12281. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. E. Hostetler, J. Michal, M. Robison, T. L. Ott, and R. L. Kincaid Effect of selenium intake and fetal age on mRNA levels of two selenoproteins in porcine fetal and maternal liver J Anim Sci, September 1, 2006; 84(9): 2382 - 2390. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. I. Biterova, A. A. Turanov, V. N. Gladyshev, and J. J. Barycki Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism PNAS, October 18, 2005; 102(42): 15018 - 15023. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Sen, R. Kopper, L. Pons, E. C. Abraham, A. W. Burks, and G. A. Bannon Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes J. Immunol., July 15, 2002; 169(2): 882 - 887. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Q.-A. Sun, L. Kirnarsky, S. Sherman, and V. N. Gladyshev Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems PNAS, March 16, 2001; (2001) 51454398. [Abstract] [Full Text]
|
|
|
|
 |
|
 B. W. Lennon, C. H. Williams Jr., and M. L. Ludwig Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase Science, August 18, 2000; 289(5482): 1190 - 1194. [Abstract] [Full Text]
|
|
|
|
 |
|
 W. K. Ray, G. Zeng, M. B. Potters, A. M. Mansuri, and T. J. Larson Characterization of a 12-Kilodalton Rhodanese Encoded by glpE of Escherichia coli and Its Interaction with Thioredoxin J. Bacteriol., April 15, 2000; 182(8): 2277 - 2284. [Abstract] [Full Text]
|
|
|
|
 |
|
 S. Gromer, L. D. Arscott, C. H. Williams Jr., R. H. Schirmer, and K. Becker Human Placenta Thioredoxin Reductase. ISOLATION OF THE SELENOENZYME, STEADY STATE KINETICS, AND INHIBITION BY THERAPEUTIC GOLD COMPOUNDS J. Biol. Chem., August 7, 1998; 273(32): 20096 - 20101. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Mora-Garcia, R. Rodriguez-Suarez, and R. A. Wolosiuk Role of Electrostatic Interactions on the Affinity of Thioredoxin for Target Proteins. RECOGNITION OF CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE BY MUTANT ESCHERICHIA COLI THIOREDOXINS J. Biol. Chem., June 26, 1998; 273(26): 16273 - 16280. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. O. Sablin and R. R. Ramsay Monoamine Oxidase Contains a Redox-active Disulfide J. Biol. Chem., June 5, 1998; 273(23): 14074 - 14076. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. B. delCardayre, K. P. Stock, G. L. Newton, R. C. Fahey, and J. E. Davies Coenzyme A Disulfide Reductase, the Primary Low Molecular Weight Disulfide Reductase from Staphylococcus aureus. PURIFICATION AND CHARACTERIZATION OF THE NATIVE ENZYME J. Biol. Chem., March 6, 1998; 273(10): 5744 - 5751. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T.-W. Gilberger, R. D. Walter, and S. Muller Identification and Characterization of the Functional Amino Acids at the Active Site of the Large Thioredoxin Reductase from Plasmodium falciparum J. Biol. Chem., November 21, 1997; 272(47): 29584 - 29589. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. B. Buchanan, C. Adamidi, R. M. Lozano, B. C. Yee, M. Momma, K. Kobrehel, R. Ermel, and O. L. Frick Thioredoxin-linked mitigation of allergic responses to wheat PNAS, May 13, 1997; 94(10): 5372 - 5377. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. D. Arscott, S. Gromer, R. H. Schirmer, K. Becker, and C. H. Williams Jr. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli PNAS, April 15, 1997; 94(8): 3621 - 3626. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Krnajski, T.-W. Gilberger, R. D. Walter, and S. Muller Intersubunit Interactions in Plasmodium falciparum Thioredoxin Reductase J. Biol. Chem., December 22, 2000; 275(52): 40874 - 40878. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. J. Raftery, Z. Yang, S. M. Valenzuela, and C. L. Geczy Novel Intra- and Inter-molecular Sulfinamide Bonds in S100A8 Produced by Hypochlorite Oxidation J. Biol. Chem., August 31, 2001; 276(36): 33393 - 33401. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Q.-A. Sun, L. Kirnarsky, S. Sherman, and V. N. Gladyshev Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems PNAS, March 27, 2001; 98(7): 3673 - 3678. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Zhong, E. S. J. Arner, and A. Holmgren Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence PNAS, May 23, 2000; 97(11): 5854 - 5859. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
