Experts and Doctors on oxidation reduction in Ann Arbor, Michigan, United States

Summary

Locale: Ann Arbor, Michigan, United States
Topic: oxidation reduction

Top Publications

  1. Tan J, Bardwell J. Key players involved in bacterial disulfide-bond formation. Chembiochem. 2004;5:1479-87 pubmed
  2. Trimmer E, Ballou D, Ludwig M, Matthews R. Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry. 2001;40:6216-26 pubmed
    ..The mutant enzyme was able to bind CH(3)-H(4)folate, but reduction of the FAD cofactor was not observed. In the NADH-menadione oxidoreductase assay, the mutant demonstrated a 240-fold decrease in activity. ..
  3. Quan S, Schneider I, Pan J, Von Hacht A, Bardwell J. The CXXC motif is more than a redox rheostat. J Biol Chem. 2007;282:28823-33 pubmed
    ..Our results indicate that the CXXC motif has the remarkable ability to confer a large number of very specific properties on thioredoxin-related proteins. ..
  4. Leonard S, Reddie K, Carroll K. Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem Biol. 2009;4:783-99 pubmed publisher
    ..The combination of selective chemical enrichment and live-cell compatibility makes DAz-2 a powerful new tool with the potential to reveal new regulatory mechanisms in signaling pathways and identify new therapeutic targets. ..
  5. Parkinson C, Liang M, Yung Y, Kirschivnk J. Habitability of enceladus: planetary conditions for life. Orig Life Evol Biosph. 2008;38:355-69 pubmed publisher
  6. Song B, Scheuner D, Ron D, Pennathur S, Kaufman R. Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes. J Clin Invest. 2008;118:3378-89 pubmed publisher
    ..These findings suggest that CHOP is a fundamental factor that links protein misfolding in the ER to oxidative stress and apoptosis in beta cells under conditions of increased insulin demand. ..
  7. Puig S, Lee J, Lau M, Thiele D. Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake. J Biol Chem. 2002;277:26021-30 pubmed
    ..Together, these results support a fundamentally conserved mechanism for high affinity copper uptake through the Ctr proteins in yeast and humans. ..
  8. Drummond J, Loo R, Matthews R. Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase. Biochemistry. 1993;32:9282-9 pubmed
  9. Pan J, Sliskovic I, Bardwell J. Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. J Mol Biol. 2008;377:1433-42 pubmed publisher
    ..Our mutants in DsbB may act by redirecting oxidant flow to take place through the isomerization pathway. ..

More Information

Publications62

  1. Ishizaki E, Fukumoto M, Puro D. Functional K(ATP) channels in the rat retinal microvasculature: topographical distribution, redox regulation, spermine modulation and diabetic alteration. J Physiol. 2009;587:2233-53 pubmed publisher
  2. Jakob U, Muse W, Eser M, Bardwell J. Chaperone activity with a redox switch. Cell. 1999;96:341-52 pubmed
    ..In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress. ..
  3. Huang H, Arscott L, Ballou D, Williams C. Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster. Biochemistry. 2008;47:12769-76 pubmed publisher
    ..On the basis of our observations, it is proposed that the function of Glu-469' is to facilitate the positioning of His-464' toward the interchange thiol, Cys-57, as suggested for the analogous residue in glutathione reductase. ..
  4. Zhang H, Gruenke L, Arscott D, Shen A, Kasper C, Harris D, et al. Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase. Biochemistry. 2003;42:11594-603 pubmed
  5. Keller P, Petrie J, De Rose P, Gerin I, Wright W, Chiang S, et al. Fat-specific protein 27 regulates storage of triacylglycerol. J Biol Chem. 2008;283:14355-65 pubmed publisher
    ..g. homeostasis model assessment). Together, these data indicate that FSP27 binds to lipid droplets and regulates their enlargement. ..
  6. Swaroop M, Bian J, Aviram M, Duan H, Bisgaier C, Loo J, et al. Expression, purification, and biochemical characterization of SAG, a ring finger redox-sensitive protein. Free Radic Biol Med. 1999;27:193-202 pubmed
    ..These results, along with our previous observations, suggest that SAG is an intracellular antioxidant molecule that may act as a redox sensor to buffer oxidative-stress induced damage. ..
  7. Hoover D, Ludwig M. A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution. Protein Sci. 1997;6:2525-37 pubmed
    ..Structural comparisons with flavodoxins from Synechococcus PCC 7942 and Anaebaena PCC 7120 suggest other residues that may also be critical for recognition by methionine synthase. ..
  8. Lee S, Im J, DiSpirito A, Bodrossy L, Barcelona M, Semrau J. Effect of nutrient and selective inhibitor amendments on methane oxidation, nitrous oxide production, and key gene presence and expression in landfill cover soils: characterization of the role of methanotrophs, nitrifiers, and denitrifiers. Appl Microbiol Biotechnol. 2009;85:389-403 pubmed publisher
    ..Collectively, these data suggest that methanotrophs expressing pMMO played a role in nitrous oxide production in these microcosms...
  9. Ortiz Maldonado M, Gatti D, Ballou D, Massey V. Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins. Biochemistry. 1999;38:16636-47 pubmed
  10. Jakob U, Eser M, Bardwell J. Redox switch of hsp33 has a novel zinc-binding motif. J Biol Chem. 2000;275:38302-10 pubmed
    ..This ionization may allow for the fast and successful activation of the chaperone function of Hsp33 upon incubation in oxidizing agents. ..
  11. Yan Z, Garg S, Kipnis J, Banerjee R. Extracellular redox modulation by regulatory T cells. Nat Chem Biol. 2009;5:721-3 pubmed publisher
    ..Regulatory T cells inhibit this redox metabolite signaling pathway, which represents a previously unrecognized mechanism for immunosuppression of effector T cells. ..
  12. Palfey B, Entsch B, Ballou D, Massey V. Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp. Biochemistry. 1994;33:1545-54 pubmed
  13. Cremers C, Reichmann D, Hausmann J, Ilbert M, Jakob U. Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone. J Biol Chem. 2010;285:11243-51 pubmed publisher
  14. Leichert L, Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol. 2004;2:e333 pubmed
    ..Remarkably, a number of these proteins were previously or are now shown to be redox regulated. ..
  15. Ren G, Stephan D, Xu Z, Zheng Y, Tang D, Harrison R, et al. Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem. 2009;284:10150-9 pubmed publisher
    ..It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins. ..
  16. Palfey B, Bjornberg O, Jensen K. Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase obtained by rapid reaction studies. Biochemistry. 2001;40:4381-90 pubmed
    ..The reduced enzyme-orotate complex reacted rapidly with menadione (180 s(-1)), demonstrating that the reduced enzyme-orotate complex is a catalytically competent intermediate. ..
  17. Graf P, Martinez Yamout M, VanHaerents S, Lilie H, Dyson H, Jakob U. Activation of the redox-regulated chaperone Hsp33 by domain unfolding. J Biol Chem. 2004;279:20529-38 pubmed
    ..This then leads to the formation of active Hsp33 dimers, which are capable of protecting cells against the severe consequences of oxidative heat stress. ..
  18. Regeimbal J, Gleiter S, Trumpower B, Yu C, Diwakar M, Ballou D, et al. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc Natl Acad Sci U S A. 2003;100:13779-84 pubmed
    ..We propose a simple model for the action of DsbB where a quinhydrone-like complex plays a crucial role as a reaction intermediate. ..
  19. Winter J, Ilbert M, Graf P, Ozcelik D, Jakob U. Bleach activates a redox-regulated chaperone by oxidative protein unfolding. Cell. 2008;135:691-701 pubmed publisher
    ..They suggest that the antimicrobial effects of bleach are largely based on HOCl's ability to cause aggregation of essential bacterial proteins. ..
  20. Davioud Charvet E, McLeish M, Veine D, Giegel D, Arscott L, Andricopulo A, et al. Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity. Biochemistry. 2003;42:13319-30 pubmed
    ..On the basis of results with chemically distinct Mannich bases, a detailed mechanism for the inactivation of TrxR is proposed...
  21. Kabil O, Banerjee R. Redox biochemistry of hydrogen sulfide. J Biol Chem. 2010;285:21903-7 pubmed publisher
    ..This report focuses on the biochemistry of H(2)S biogenesis and clearance, on the molecular mechanisms of its action, and on its varied biological effects. ..
  22. Ahn S, Thiele D. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes Dev. 2003;17:516-28 pubmed
    ..This redox-dependent activation of HSF1 by heat and hydrogen peroxide establishes a common mechanism in the stress activation of Hsp gene expression by mammalian HSF1. ..
  23. Collet J, D Souza J, Jakob U, Bardwell J. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J Biol Chem. 2003;278:45325-32 pubmed
    ..The zinc-free protein conserves its reductase activity. Altogether, our results suggest that the zinc center might play the role of a redox switch, changing a yet to be identified activity. ..
  24. Desrochers P, Mookhtiar K, Van Wart H, Hasty K, Weiss S. Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases. J Biol Chem. 1992;267:5005-12 pubmed
    ..These data demonstrate that human neutrophils use chlorinated oxidants to activate collagenolytic metalloproteinases whose substrate specificities can be extended to members of the serpin superfamily. ..
  25. Bauer H, Massey V, Arscott L, Schirmer R, Ballou D, Williams C. The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster. J Biol Chem. 2003;278:33020-8 pubmed
    ..Additional data suggest that Cys57 attacks Cys490' in the interchange reaction between the N-terminal dithiol and the C-terminal disulfide. ..
  26. Snider N, Walker V, Hollenberg P. Oxidation of the endogenous cannabinoid arachidonoyl ethanolamide by the cytochrome P450 monooxygenases: physiological and pharmacological implications. Pharmacol Rev. 2010;62:136-54 pubmed publisher
  27. Dixon M, Huang S, Matthews R, Ludwig M. The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12. Structure. 1996;4:1263-75 pubmed
    ..The catalytic and activation cycles may be turned off and on by alternating physical separation and approach of the reactants. ..
  28. Paulsen C, Carroll K. Chemical dissection of an essential redox switch in yeast. Chem Biol. 2009;16:217-25 pubmed publisher
  29. Hopkins N, Williams C. Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Biochemistry. 1995;34:11757-65 pubmed
    ..However, the FAD of C44S is markedly less completely reduced by 1 equiv of NADH than is the FAD of C49S. Ferricyanide stoichiometrically reoxidizes the FADH2 of both altered forms of the enzyme. ..
  30. Hopkins N, Williams C. Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides. Biochemistry. 1995;34:11766-76 pubmed
    ..Fluorescence and absorbance spectrophotometry were used to determine the binding of NAD+ to the oxidized forms of the enzymes as 275 microM and 270 microM for C44S and C49S, respectively. ..
  31. Yan Z, Banerjee R. Redox remodeling as an immunoregulatory strategy. Biochemistry. 2010;49:1059-66 pubmed publisher
    ..The role of regulatory T cells in perturbing redox remodeling by dendritic cells and its implications as a general regulatory T cell suppression mechanism are discussed...
  32. Koutmos M, Datta S, Pattridge K, Smith J, Matthews R. Insights into the reactivation of cobalamin-dependent methionine synthase. Proc Natl Acad Sci U S A. 2009;106:18527-32 pubmed publisher
  33. Jarrett J, Choi C, Matthews R. Changes in protonation associated with substrate binding and Cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry. 1997;36:15739-48 pubmed
    ..In contrast, binding methyltetrahydrofolate to the enzyme does not result in proton uptake, suggesting that the proton destined for the product tetrahydrofolate is already present on the free methylcobalamin enzyme. ..
  34. Zander T, Phadke N, Bardwell J. Disulfide bond catalysts in Escherichia coli. Methods Enzymol. 1998;290:59-74 pubmed
  35. Rider L, Ottosen M, Gattis S, Palfey B. Mechanism of dihydrouridine synthase 2 from yeast and the importance of modifications for efficient tRNA reduction. J Biol Chem. 2009;284:10324-33 pubmed publisher
    ..Dihydrouridine of modified tRNA from Escherichia coli was also oxidized to uridine showing the reaction to be reversible. ..
  36. Trimmer E, Ballou D, Matthews R. Methylenetetrahydrofolate reductase from Escherichia coli: elucidation of the kinetic mechanism by steady-state and rapid-reaction studies. Biochemistry. 2001;40:6205-15 pubmed
    ..We conclude that studies of individual half-reactions catalyzed by E. coli MTHFR may be used to probe mechanistic questions relevant to the overall oxidoreductase reactions. ..
  37. Graf P, Jakob U. Redox-regulated molecular chaperones. Cell Mol Life Sci. 2002;59:1624-31 pubmed
  38. Ortiz Maldonado M, Entsch B, Ballou D. Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis. Biochemistry. 2004;43:15246-57 pubmed publisher
    ..1, indicating the involvement of the H-bond network. We conclude that product deprotonation enhances the rate of a specific conformational change required for both product release and the elimination of water from C4a-OH-FAD...
  39. Karow D, Pan D, Davis J, Behrends S, Mathies R, Marletta M. Characterization of functional heme domains from soluble guanylate cyclase. Biochemistry. 2005;44:16266-74 pubmed
    ..003/min at 37 degrees C. This paper has identified and characterized the minimum functional ligand-binding heme domain derived from sGC, providing key details toward a comprehensive characterization. ..
  40. Bader M, Hiniker A, Regeimbal J, Goldstone D, Haebel P, Riemer J, et al. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBO J. 2001;20:1555-62 pubmed
    ..Our results suggest that dimerization acts to protect DsbC's active sites from DsbB-mediated oxidation. These results explain how oxidative and reductive pathways can co-exist in the periplasm of Escherichia coli. ..
  41. Ortiz Maldonado M, Ballou D, Massey V. A rate-limiting conformational change of the flavin in p-hydroxybenzoate hydroxylase is necessary for ligand exchange and catalysis: studies with 8-mercapto- and 8-hydroxy-flavins. Biochemistry. 2001;40:1091-101 pubmed
    ..Presumably, the protein environment surrounding the flavin in Eox* differs slightly from that of the final resting form of the enzyme (Eox). ..
  42. Hondorp E, Matthews R. Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli. J Bacteriol. 2009;191:3407-10 pubmed publisher
  43. Jeong H, Hayes K. Reductive dechlorination of tetrachloroethylene and trichloroethylene by mackinawite (FeS) in the presence of metals: reaction rates. Environ Sci Technol. 2007;41:6390-6 pubmed
    ..The dechlorination rates of PCE and TCE significantly varied with Fe(ll) amendment concentrations (Fe(II)0), indicating the presence of different types of solid-bound Fe phases with Fe(II)o. ..
  44. Shao F, Bader M, Jakob U, Bardwell J. DsbG, a protein disulfide isomerase with chaperone activity. J Biol Chem. 2000;275:13349-52 pubmed
    ..DsbG is one of the first periplasmic proteins shown to have general chaperone activity. This ability to chaperone protein folding is likely to increase the effectiveness of DsbG as a protein disulfide isomerase. ..
  45. Lennon B, Williams C, Ludwig M. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science. 2000;289:1190-4 pubmed
    ..Comparison of these structures demonstrates that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees...
  46. Regeimbal J, Bardwell J. DsbB catalyzes disulfide bond formation de novo. J Biol Chem. 2002;277:32706-13 pubmed
    ..These unexpected findings raise the possibility that the oxidation of DsbA by DsbB does not occur via thiol disulfide exchange as is widely assumed but rather, directly via quinone reduction. ..
  47. Deshpande R, Woods T, Fu J, Zhang T, Stoll S, Elder J. Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking. J Invest Dermatol. 2000;115:477-85 pubmed
    ..Based on these findings, we propose that S100A2 may protect normal keratinocytes against carcinogens by participating in the cellular proof-reading response to oxidative stress. ..
  48. Bader M, Muse W, Ballou D, Gassner C, Bardwell J. Oxidative protein folding is driven by the electron transport system. Cell. 1999;98:217-27 pubmed
    ..Under truly anaerobic conditions, menaquinone shuttles electrons to alternate final electron acceptors such as fumarate. This flexibility reflects the vital nature of the disulfide catalytic system. ..
  49. Schenk S, Horowitz J. Coimmunoprecipitation of FAT/CD36 and CPT I in skeletal muscle increases proportionally with fat oxidation after endurance exercise training. Am J Physiol Endocrinol Metab. 2006;291:E254-60 pubmed
    ..857, P < 0.003). In conclusion, the findings from this study indicate that exercise training alters the localization of FAT/CD36 and increases its association with CPT I, which may help augment fat oxidation. ..
  50. Williams C. Mechanism and structure of thioredoxin reductase from Escherichia coli. FASEB J. 1995;9:1267-76 pubmed
    ..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. ..
  51. Cole L, Gatti D, Entsch B, Ballou D. Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase. Biochemistry. 2005;44:8047-58 pubmed
    ..This work demonstrates some general principles of how enzymes use conformational movements to allow both access and egress of substrates and product, while restricting access to the solvent at a critical stage in catalysis. ..
  52. Miller J, Busby R, Jordan S, Cheek J, Henshaw T, Ashley G, et al. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry. 2000;39:15166-78 pubmed
    ..These results provide information about the mechanism of LipA catalysis and place LipA within the family of iron-sulfur proteins that utilize AdoMet for radical-based chemistry. ..
  53. Leiser S, Miller R. Nrf2 signaling, a mechanism for cellular stress resistance in long-lived mice. Mol Cell Biol. 2010;30:871-84 pubmed publisher
    ..Augmented activity of Nrf2 and ARE-responsive genes may coordinate many of the stress resistance traits seen in cells from these long-lived mutant mice. ..