A survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: Implications for ros production, cancer etiology, and neurodegenerative diseases

Advances in Enzymology and Related Areas of Molecular Biology

Volumn 77 1, Issue , 2010, Pages 307-360

  Bunik, Victoria I ^a   Schloss, John V ^b   Pinto, John T ^c   Dudareva, Natalia ^d   Cooper, Arthur J L ^c  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b UNIVERSITY OF NEW ENGLAND   (United States)

^c NEW YORK MEDICAL COLLEGE   (United States)

^d PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; ALPHA-KETOGLUTARIC ACID; ANION; AROMATIC LEVO AMINO ACID DECARBOXYLASE; CARBON; ENZYME; OXYGEN; REACTIVE OXYGEN METABOLITE;

ANIMAL; CATALYSIS; CHEMICAL MODEL; CHEMISTRY; DEGENERATIVE DISEASE; HUMAN; METABOLISM; NEOPLASM; REVIEW;

ANIMALS; ANIONS; AROMATIC-L-AMINO-ACID DECARBOXYLASES; CARBON; CATALYSIS; ENZYMES; HUMANS; KETOGLUTARIC ACIDS; MODELS, CHEMICAL; NEOPLASMS; NEURODEGENERATIVE DISEASES; OXYGEN; REACTIVE OXYGEN SPECIES;

EID: 79960957262     PISSN: 0065258X     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article

References (126)

1. Healy, M. J., and Christen, P. (1972) Reaction of the carbanionic aldolase-substrate intermediate with tetranitromethane: identification of the products, hydroxypyruvaldehyde phosphate and D-5-ketofructose 1,6-diphosphate, J. Am. Chem. Soc. 94, 7911-7916.
2. Healy, M. J., and Christen, P. (1973) Mechanistic probes for enzymatic reactions: oxidation-reduction indicators as oxidants of intermediary carbanions (studies with aldolase, aspartate aminotransferase, pyruvate decarboxylase, and 6-phosphogluconate dehydrogenase), Biochemistry 12, 35-41.
3. 2 oxidizes an aldolase dihydroxyacetone phosphate intermediate to hydroxymethylglyoxal phosphate, Experientia 30, 603-605.
4. Christen, P., and Gasser, A. (1976) Oxidation of the carbanion intermediate of transaldolase by hexacyanoferrate(III), J. Biol. Chem. 251, 4220-4223.
5. Christen, P., Cogoli-Greuter, M., Healy,M. J., and Lubini, D. (1976) Specific irreversible inhibition of enzymes concomitant to the oxidation of carbanionic enzyme- substrate intermediates by hexacyanoferrate(III), Eur. J. Biochem. 63, 223-231.
6. Christen, P. (1977) Paracatalytic enzyme modification by oxidation of enzyme- substrate carbanion intermediates, Methods Enzymol. 46, 48-54.
7. Cogoli-Greuter, M., Hausner, U., and Christen, P. (1979) Irreversible inactivation of pyruvate decarboxylase in the presence of substrate and an oxidant: an example of paracatalytic enzyme inactivation, Eur. J. Biochem. 100, 295-300.
8. 2, Eur. J. Biochem. 107, 73-77.
9. Bowes, G., and Ogren, W. L. (1972) Oxygen inhibition and other properties of soybean ribulose 1,5-diphosphate carboxylase, J. Biol. Chem. 247, 2171-2176.
10. Ryan, F. J., and Tolbert, N. E. (1975) Ribulose diphosphate carboxylase/oxygenase: III. Isolation and properties, J. Biol. Chem. 250, 4229-4233.
11. Chen, Z. X., Chastain, C. J., Al-Abed, S. R., Chollet, R., and Spreitzer, R. J. (1988) Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas, Proc. Natl. Acad. Sci. USA 85, 4696-4699.
12. Yu, G.-X., Park, B.-H., Chandramohan, P., Geist, A., and Samatova, N. F. (2005) An evolution-based analysis scheme to identify CO2/O2 specificity-determining factors for ribulose 1,5-bisphosphate carboxylase/oxygenase, Protein Eng. Des. Sel. 18, 589-596.
13. Schloss, J. V., and Hixon, M. S. (1998) Enol chemistry and enzymology, in Comprehensive Biological Catalysis, Vol. 2, Reactions of Nucleophilic/Carbanionoid Carbon, Sinnod, M., Ed., Academic Press, London, pp. 43-114.
14. Ogren, W. L. (2003) Affixing the O to Rubisco: discovering the source of photorespiratory glycolate and its regulation, Photosynth. Res. 76, 53-63.
15. Abell, L. M., and Schloss, J. V. (1991) Oxygenase side reactions of acetolactate synthase and other carbanion-forming enzymes, Biochemistry 30, 7883-7887.
16. Hixon, M., Sinerius, G., Schneider, A., Walter, C., Fessner, W.-D., and Schloss, J. V. (1996) Quo vadis photorespiration: a tale of two aldolases, FEBS Lett. 392, 281-284.
17. Fessner,W.-D., Schneider, A., Held, H., Sinerius, G.,Walter, C., Hixon, M., and Schloss, J. V. (1996) The mechanism of class II, metal-dependent aldolases, Angew. Chem. Int. Ed. Engl. 35, 2219-2221.
18. Duggleby, R. G., McCourt, J. A., and Guddat, L. W. (2008) Structure and mechanism of inhibition of plant acetohydroxyacid synthase, Plant Physiol. Biochem. 46, 309-324.
19. Hixon, M. S. (1997) Oxygen consuming side reactions of carbanion forming enzymes: the accidental oxygenases, Ph.D. dissertation, University of Kansas.
20. Tse, J. M.-T., and Schloss, J. V. (1993) The oxygenase reaction of acetolactate synthase, Biochemistry 32, 10398-10403.
21. Lubini, D. G. E., and Christen, P. (1979) Paracatalytic modification of aldolase: a side reaction of the catalytic cycle resulting in irreversible blocking of two active-site lysyl residues, Proc. Natl. Acad. Sci. USA 76, 2527-2531.
22. Schloss, J. V. (1984) Interaction of the herbicide sulfometuron methyl with acetolactate synthase: a slow-binding inhibitor, in Flavins and Flavoproteins, Bray, R. C., Engel, P. C., and Mayhew, S. G., Eds., Walter de Gruyter, New York, pp. 737-740.
23. Schloss, J. V., Ciskanik, L., Pai, E. F., and Thorpe, C. (1991) Acetolactate synthase: a deviant flavoprotein, in Flavins and Flavoproteins, Curti, B., Ronchi, S., and Zanetti, G., Eds., Walter de Gruyter, New York, pp. 907-914.
24. Tittmann, K., Schrcoder, K., Golbik, R., McCourt, J., Kaplun, A., Duggleby, R. G., Barak, Z., Chipman, D. M., and Hcubner, G. (2004) Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of (a-hydroxyethyl)thiamin diphosphate in a " nonredox" flavoenzyme, Biochemistry 43, 8652-8661.
25. Schloss, J. V., Hixon, M. S., Chu, F., Chang, S., and Duggleby, R. G. (1996) Products formed in the oxygen-consuming reactions of acetolactate synthase and pyruvate decarboxylase, in Biochemistry and Physiology of Thiamin Diphosphate Enzymes, Bisswanger, H., and Schellenberger, A., Eds., Intemann, Prien, Germany, pp. 580-585.
26. Grabau, C., and Cronan, J. E., Jr. (1986) Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein, Nucleic Acids Res. 14, 5449-5460.
27. Schloss, J. V., Ciskanik, L. M., and Van Dyk, D. E. (1988) Origin of the herbicide binding site of acetolactate synthase, Nature 331, 360-362.
28. J. V. Schloss (E.I. Du Pont de Nemours & Co.), unpublished work, 1984.
29. Schloss, J. V. (1994) Recent advances in understanding the mechanism and inhibition of acetolactate synthase, in Chemistry of Plant Protection, Vol. 10, Stetter, J., Ed., Springer-Verlag, Berlin, pp. 3-14.
30. Ibdah, M., Bar-Ilan, A., Livnah, O., Schloss, J. V., Barak, Z., and Chipman, D. M. (1996) Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis, Biochemistry 35, 16282-16291.
31. McCourt, J. A., Pang, S. S., Guddat, L. W., and Duggleby, R. G. (2005) Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase, Biochemistry 44, 2330-2338.
32. McCourt, J. A., Pang, S. S., King-Scott, J., Guddat, L. W., and Duggleby, R. G. (2006) Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase, Proc. Natl. Acad. Sci. USA 103, 569-573.
33. Chipman, D., Barak, Z., and Schloss, J. V. (1998) Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases, Biochim. Biophys. Acta 1385, 401-419.
34. Grueninger, D., and Schulz, G. E. (2008) Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase, Biochemistry 47, 607-614.
35. Kroemer, M., and Schulz, G. E. (2002) The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging, Acta Crystallogr. D 58, 824-832.
36. Kroemer, M., Merkel, I., and Schulz, G. E. (2003) Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase, Biochemistry 42, 10560-10568.
37. Hong, J., Sun, S., Derrick, T., Larive, C., Schowen, K. B., and Schowen, R. L. (1998) Transition-state theoretical interpretation of the catalytic power of pyruvate decarboxylases: the roles of static and dynamical considerations, Biochim. Biophys. Acta 1385, 187-200.
38. Christeller, J. T. (1981) The effects of bivalent cations on ribulose bisphosphate carboxylase/oxygenase, Biochem. J. 193, 839-844.
39. Bertoldi, M., Carbone, V., and Borri Voltattorni, C. (1999) Ornithine and glutamate decarboxylases catalyse an oxidative deamination of their a-methyl substrates, Biochem. J. 342, 509-512.
40. Chang, S. (2005) On the oxygenase activity of bacterial glutamate decarboxylase: an examination of the kinetic mechanism, Ph.D. dissertation, University of Kansas.
41. Davis, K., Foos, T., Wu, J.-Y., and Schloss, J. V. (2001) Oxygen-induced seizures and inhibition of human glutamate decarboxylase and porcine cysteine sulfinic acid decarboxylase by oxygen and nitric oxide, J. Biomed. Sci. 8, 359-364.
42. Davis, K., and Schloss, J. V. (1999) Unpublished work, University of Kansas, Lawrence, KS.
43. Schloss, J. V. (1988) Significance of slow binding enzyme inhibition and its relationship to reaction-intermediate analogues, Acc. Chem. Res. 21, 348-353.
44. Choi, S. Y., and Churchich, J. E. (1986) Glutamate decarboxylase side reactions catalyzed by the enzyme, Eur. J. Biochem. 160, 515-520.
45. Porter, T. G., and Martin, D. L. (1987) Rapid inactivation of brain glutamate decarboxylase by aspartate, J. Neurochem. 48, 67-72.
46. Li, Q., Guo, M., Xu, X., Xiao, X., Xu, W., Sun, X., Tao, H., and Li, R. (2008) Rapid decrease of GAD 67 content before the convulsion induced by hyperbaric oxygen exposure, Neurochem. Res. 33, 185-193.
47. Bertoldi, M., Moore, P. S., Maras, B., Dominici, P., and Borri Voltattorni, C. B. (1996) Mechanism-based inactivation of dopa decarboxylase by serotonin, J. Biol. Chem. 271, 23954-23959.
48. Bertoldi, M., Dominici, P., Moore, P. S., Maras, B., and Borri Voltattorni, C. B. (1998) Reaction of dopa decarboxylase with a-methyldopa leads to an oxidative deamination producing 3,4-dihydroxyphenylacetone, an active site directed affinity label, Biochemistry 37, 6552-6561.
49. Bertoldi, M., Frigeri, P., Paci, M., and Borri Voltattorni, C. B. (1999) Reaction specificity of native and nicked 3,4-dihydroxyphenylalanine decarboxylase, J. Biol. Chem. 274, 5514-5521.
50. Bertoldi, M., Gonsalvi, M., Contestabile, R., and Borri Voltattorni C. B. (2002) Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylationdependent oxidative deaminase, J. Biol. Chem. 277, 36357-36362.
51. Bertoldi, M., and Borri Voltattorni, C. (2003) Reaction and substrate specificity of recombinant pig kidney dopa decarboxylase under aerobic and anaerobic conditions, Biochim. Biophys. Acta 1647, 42-47.
52. Bertoldi, M., Cellini, B., Maras, B., and Borri Voltattorni, C. (2005) A quinonoid is an intermediate of oxidative deamination reaction catalyzed by dopa decarboxylase, FEBS Lett. 579, 5175-5180.
53. Bertoldi, M., Cellini, B., Montioli, R., and Borri Voltattorni, C. (2008) Insights into the mechanism of oxidative deamination catalyzed by dopa decarboxylase, Biochemistry 47, 7187-7195.
54. O'Leary, M. H., and Baughn, R. L. (1977) Decarboxylation-dependent transamination catalyzed by mammalian 3,4-dihydroxyphenylalanine decarboxylase, J. Biol. Chem. 252, 7168-7173.
55. Allen, G. F., Land, J. M., and Heales, S. J. (2009) A new perspective on the treatment of aromatic L-amino acid decarboxylase deficiency, Mol. Genet. Metab. 97, 6-14.
56. Sakai, K., Miyasako, Y., Nagatomo, H., Watanabe, H., Wakayama, M., and Moriguchi, M. (1997) L-Ornithine decarboxylase from Hafnia alvei has a novel L-ornithine oxidase activity, J. Biochem. 122, 961-968.
57. Kaminaga, Y., Schnepp, J., Peel, G., Kish, C. M., Ben-Nissan, G., Weiss, D., Orlova, I., Lavie, O., Rhodes, D., Wood, K., et al. (2006) Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation, J. Biol. Chem. 281, 23357-23399.
58. Kato, Y., Tsuda, Y., and Asano, Y. (2007) Purification and partial characterization of N-hydroxy-L-phenylalanine decarboxylase/oxidase from Bacillus sp. strain Ox-B1, an enzyme involved in the " aldoximine-nitrile" pathway, Biochim. Biophys. Acta 1774, 856-965.
59. Tapia, O., and Andrés, J. (1992) Towards an explanation of carboxylation/oxygenation bifunctionality in Rubisco: transition structure for the carboxylation reaction of 2,3,4-pentanetriol, J. Mol. Eng. 2, 37-41.
60. Andrés, J., Safont, V. S., and Tapia, O. (1992) Straining the double bond in 1,2-dihydroxyethylene: a simple theoretical model for the enediol moiety in Rubisco's substrate and analogs, Chem. Phys. Lett. 198, 515-520.
61. Andrés, J., Safont, V. S., Queralt, J., and Tapia, O. (1993) A theoretical study of the singlet-triplet energy gap dependence upon rotation and pyramidalization for 1,2-dihydroxyethylene: a simple model to study the enediol moiety in Rubisco's substrate, J. Phys. Chem. 97, 7888-7893.
62. 6 Pyridoxal Phosphate, Wiley, New York.
63. Amadasi, A., Bertoldi, M., Contestabile, R., Bettati, S., Cellini, B., di Salvo, M. L., Borri Voltattorni, C., Bossa, F., and Mozzarelli, A. (2007) Pyridoxal 50-phosphate enzymes as targets for therapeutic agents, Curr. Med. Chem. 14, 1291-1324.
64. Agnihotri, G., and Liu, H. W. (2001) PLP and PMP radicals: a new paradigm in coenzyme B6 chemistry, Bioorg. Chem. 29, 234-257.
65. Lepore, B. W., Ruzicka, F. J., Frey, P. A., and Ringe, D. T. (2005) The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale, Proc. Natl. Acad. Sci. USA 102, 13819-13824.
66. Berkovitch, F., Behshad, E., Tang, K. H., Enns, E. A., Frey, P. A., and Drennan, C. L. (2004) A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase, Proc. Natl. Acad. Sci. USA 101, 15870-15875.
67. Agnihotri, G., Liu, Y. N., Paschal, B. M., and Liu, H. W. (2004) Identification of an unusual [2Fe-2S]-binding motif in the CDP-6-deoxy-D-glycero-l-threo-4-hexulose-3-dehydrase from Yersinia pseudotuberculosis: implication for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses, Biochemistry 43, 14265-14274.
68. Scumegi, B., and Alkonyi, I. (1983) Paracatalytic inactivation of pig heart pyruvate dehydrogenase complex, Arch. Biochem. Biophys. 223, 417-424.
69. Frey, P. A., Flournoy, D. S., Gruys, K., and Yang, Y.-S. (1989) Intermediates in reductive transacetylation catalyzed by pyruvate dehydrogenase complex, Ann. NY Acad. Sci. 573, 21-35.
70. Graham, L. D., Packman, L. C., and Perham, R. N. (1989) Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes, Biochemistry 28, 1574-1581.
71. Bunik, V. I. (1987) Unpublished work, Lomonosov Moscow State University, Moscow, Russia.
72. Doerge, D. R., and Corbett, M. D. (1985) The action of a-ketoglutarate dehydrogenase on 4-chloronitrosobenzene: evidence for species-dependent differences in active site properties, Comp. Biochem. Physiol. 80C, 161-165.
73. Carlberg, I., and Mannervik, B. (1980) Interaction of 2,4,6-trinitrobenzenesulfonate and 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole with the active sites of glutathione reductase and lipoamide dehydrogenase, Acta Chem. Scand. B 34, 144-146.
74. Bunik, FV. I., and Gomazkova, V. S. (1996) Study of 2-oxoglutarate dehydrogenase by the method of chemical modification of amino acid residues, in Chemical Modification of Enzymes, Kurganov, B. I., Nagradova, N. K., and Lavrik, O. I., Eds., Nova Science Publishers, New York, pp. 479-521.
75. Corbett, M. D., and Chipko, B. R. (1980) Comparative aspects of hydroxamic acid production by thiamine-dependent enzymes, Bioorg. Chem. 9, 273-287.
76. Corbett, M. D., Corbett, B. R., and Doerge, D. R. (1982) Hydroxamic production and active-site induced Bamberger rearrangement from the action of a-ketoglutarate dehydrogenase on 4-chloronitrosobenzene, J. Chem. Soc. Perkin Trans. I 345-350.
77. Corbett, M. D., Doerge, D. R., and Corbett, B. R. (1983) Hydroxamic acid production by a-ketoglutarate dehydrogenase: 2. Evidence for an electrophilic reaction intermediate at the enzyme active site, J. Chem. Soc. Perkin Trans. I 765-769.
78. Bunik, V. I., and Pavlova, O. G. (1997) Inactivation of a-ketoglutarate dehydrogenase during its enzymatic reaction, Biochemistry (Moscow) 62, 973-982.
79. Frank, R. A. W., Kay, C. W. M., Hirst, J., and Luisis, B. F. (2008) Off-pathway oxygendependent thiamine radical in the Krebs cycle, J. Am. Chem. Soc. 130, 1662-1668.
80. Bunik,V. I., and Sievers,C. (2002) Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species, Eur. J. Biochem. 269, 5004-5015.
81. Bunik, V. (2000) Increased catalytic performance of the 2-oxoacid dehydrogenase complexes in the presence of thioredoxin, a thiol-disulfide oxidoreductase, J. Mol. Catal. B 8, 165-174.
82. Bunik, V. I. (2003) 2-Oxo acid dehydrogenase complexes in redox regulation, Eur. J. Biochem. 270, 1036-1042.
83. Bunik, V., Raddatz, G., Lemaire, S., Meyer, Y., Jacquot, J.-P., and Bisswanger, H. (1999) Interaction of thioredoxins with target proteins: role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes, Protein Sci. 8, 65-74.
84. Starkov, A. A., Fiskum, G., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., and Beal, M. F. (2004) Mitochondrial a-ketoglutarate dehydrogenase complex generates reactive oxygen species, J. Neurosci. 24, 7779-7788.
85. Tretter, L., and Adam-Vizi, V. (2004) Generation of reactive oxygen species in the reaction catalyzed by a-ketoglutarate dehydrogenase, J. Neurosci. 24, 7771-7778.
86. Zcundorf, G., Kahlert, S., Bunik, V. I., and Reiser, G. (2009) a-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ, Neuroscience 158, 610-616.
87. Bunik, V. I. (1989) Unpublished work, Lomonosov Moscow State University, Moscow, Russia.
88. Pavlova, O. G. (1996) Interaction of a-ketoglutarate dehydrogenase from pigeon breast muscle with the a-keto substrate and its structural analogs, Ph.D. dissertation, Lomonosov Moscow State University, Moscow, Russia.
89. Kedderis, G. L., and Hollenberg, P. F. (1983) Characterization of the N-demethylation reactions catalyzed by horseradish peroxidase, J. Biol. Chem. 258, 8129-8138.
90. Schonbaum, G. R., and Lo, S. (1972) Interaction of peroxidases with aromatic peracids and alkyl peroxides. Product analysis, J. Biol. Chem. 247, 3353-3360.
91. Varfolomeev, S. D. (1984) Enzyme inactivation in the reaction process. Regulatory role [Russian], Biokhimiia 49, 723-735.
92. Sud'ina, G. F., Kobel'kov, G. M., and Varfolomeev, S. D. (1987) The macrokinetic behavior of an enzymatic system with an enzyme inactivated in the reaction, Biotechnol. Bioeng. 29, 625-632.
93. Davidson, V. L. (2007) Protein-derived cofactors. Expanding the scope of post-translational modifications, Biochemistry 46, 5283-5292.
94. Burke, W. J., Li, S. W., Williams, E. A., Nonneman, R., and Zahm, D. S. (2003) 3,4-Dihydroxyphenylacetaldehyde is the toxic dopamine metabolite in vivo: implications for Parkinson's disease pathogenesis, Brain Res. 989, 205-213.
95. Finefrock, A. E., Bush, A. I., and Doraiswamy, P. M. (2003) Current status of metals as therapeutic targets in Alzheimer's disease, J. Am. Geriatr. Soc. 51, 1143-1148.
96. Gazaryan, I. G., Krasnikov, B. F., Ashby, G. A., Thorneley, R. N. F., Kristal, B. S., and Brown, A. M. (2002) Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase, J. Biol. Chem. 277, 10064-10072.
97. Corbett, M. D., and Corbett, B. R. (1986) Effect of ring substituents on the transketolasecatalyzed conversion of nitroso aromatics to hydroxamic acids, Biochem. Pharmacol. 35, 3613-3621.
98. Yoshioka, T., and Uematsu, T. (1998) Biotransformation of nitroso aromatic compounds and 2-oxo acids to N-hydroxy-N-arylacylamides by thiamine-dependent enzymes in rat liver, Drug Metab. Dispos. 26, 705-710.
99. Yoshioka, T., Ohno, H., and Uematsu, T. (1996) Pyruvate dehydrogenase complexcatalyzed formation of N-arylacetohydroxamic acids from nitroso aromatic compounds in rat isolated cells and perfused organs, J. Pharmacol. Exp. Ther. 279, 1282-1289.
100. Ferguson, L. R. (2002) Natural and human-made mutagens and carcinogens in the human diet, Toxicology 181-182, 79-82.
101. Kangsadalampai, K., Butryee, C., and Manoonphol, K. (1997) Direct mutagenicity of the polycylic aromatic hydrocarbon-containing fraction of smoked and charcoal-broiled foods treated with nitrite in acid solution, Food Chem. Toxicol. 35, 213-218.
102. Yang, D., Tannenbaum, S. R., Büchi, G., and Lee, G. C. (1984) 4-Chloro-6-methoxyindole is the precursor of a potent mutagen (4-chloro-6-methoxy-2-hydroxy-1-nitrosoindolin-3-one oxime) that forms during nitrosation of the fava bean (Vicia faba), Carcinogenesis 5, 1219-1224.
103. Ivankovic, S., Seibel, J., Komitowski, D., Spiegelhalder, B., Preussmann, R., and Siddiqi, M. (1998) Caffeine-derived N-nitroso compounds: V. Carcinogenicity of mononitrosocaffeidine and dinitrosocaffeidine in bd-ix rats, Carcinogenesis 19, 933-937.
104. Lin, J. K., Wu, S. S., and Chen, J. T. (1986) Mutagenicities of nitrosated carboline derivatives, Proc. Natl. Sci. Counc. Repub. China B 10, 280-286.
105. Tricker, A. R., Pfundstein, B., Kälble, T., and Preussmann, R. (1992) Secondary amine precursors to nitrosamines in human saliva, gastric juice, blood, urine and faeces, Carcinogenesis 13, 563-568.
106. Kumano, T., Yoshioka, T., and Uematsu, T. (1986) Comparative effect of chemical structure of chlorinated N-hydroxy-N-acyl-aminobiphenyl ethers and their related compounds on rat liver cytosol-catalyzed transacylation, Drug Metab. Dispos. 14, 487-493.
107. Gibson, G. E., Blass, J. P., Beal, M. F., and Bunik, V. (2005) The a-ketoglutaratedehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration, Mol. Neurobiol. 31, 43-63.
108. Ko, L. W., Sheu, K. F.-R., Thaler, H. T., Markesbery, W. R., and Blass, J. P. (2001) Selective loss of KGDHC-enriched neurons in Alzheimer temporal cortex: Does mitochondrial variation contribute to selective vulnerability? J. Mol. Neurosci. 17, 361-369.
109. Hefti, F., and Weiner, W. J. (1986) Nerve growth factor and Alzheimer's disease, Ann. Neurol. 20, 275-281.
110. Butterworth, R. F., and Leong, D. K. (1996) Thiamine deficiency (Wernicke's) encephalopathy: pathophysiologic mechanisms and development of positron emission tomography (PET) ligands, in Biochemistry and Physiology of Thiamin Diphosphate Enzymes, Bisswanger, H., and Schellenberger, A., Eds., Intemann, Prien, Germany, pp. 409-417.
111. Venkatraman, A., Landar, A., Davis, A. J., Chamlee, L., Sanderson, T., Kim, H., Page, G., Pompilius, M., Ballinger, S., Darley-Usmar, V., and Bailey, S. M. (2004) Modification of the mitochondrial proteome in response to the stress of ethanol-dependent hepatotoxicity, J. Biol. Chem. 279, 22092-22101.
112. Kabysheva, M. S., Storozhevykh, T. P., Pinelis V. G., and Bunik V. I. (2009) Synthetic regulators of the 2-oxoglutarate oxidative decarboxylation alleviate the glutamate excitotoxicity in cerebellar granule neurons, Biochem. Pharmacol. 77, 1531-1540.
113. Graf, A., Kabysheva, M., Klimuk, E., Trofimova, L., Dunaeva, T., Zundorf, G., Kahlert, S., Reiser, G., Storozhevykh, T., Pinelis, V., et al. (2009) Role of 2-oxoglutarate dehydrogenase in brain pathologies involving glutamate neurotoxicity, J. Mol. Catal. B61, 60, 80-87.
114. Kahlert, S., Zündorf, G., and Reiser, G. (2005) Glutamate-mediated influx of extracellular Ca2{thorn} is coupled with reactive oxygen species generation in cultured hippocampal neurons but not in astrocytes, J. Neurosci. Res. 79, 262-271.
115. Bunik, V. I., Denton, T. T., Xu, H., Thompson, C. M., Cooper, A. J. L., and Gibson, G. E. (2005) Phosphonate analogues of a-ketoglutarate inhibit the activity of the a-ketoglutarate dehydrogenase complex isolated from brain and in cultured cells, Biochemistry 44, 10552-10561.
116. Bunik, V., Kaehne, T., Degtyarev, D., Shcherbakova, T., and Reiser, G. (2008) Novel isoform of 2-oxogluratate dehydrogenase is identified in brain, but not in heart, FEBS J. 275, 4990-5006.
117. Bunik, V. I., and Degtyarev, D. (2008) Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins, Proteins 71, 874-890.
118. McCartney, R. G., Rice, J. E., Sanderson, S., Bunik, V., Lindsay, H., and Lindsay, J. G. (1998) Subunit interactions in the mammalian a-ketoglutarate dehydrogenase complex: evidence for direct association of the a-ketoglutarate dehydrogenase (E1) and dihydrolipoamide dehydrogenase (E3) components, J. Biol. Chem. 273, 24158-24164.
119. MacDonald, M. J., Husain, R. D., Hoffmann-Benning, S., and Baker, T. R. (2004) Immunochemical identification of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the a-ketoglutarate and pyruvate dehydrogenase complexes partially explains the cellular toxicity of coenzyme Q0, J. Biol. Chem. 279, 27278-27285.
120. Elam, J. S., Malek, K., Rodriguez, J. A., Doucette, P. A., Taylor, A. B., Hayward, L. J., Cabelli, D. E., Valentine, J. S., and Hart, P. J. (2003) An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate, J. Biol. Chem. 278, 21032-21039.
121. Liochev, S. I., and Fridovich, I. (2004) Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions, Proc. Natl. Acad. Sci. USA 101, 12485-12490.
122. Andrekopoulos, C., Zhang, H., Joseph, J., Kalivendi, S., and Kalyanaraman, B. (2004) Bicarbonate enhances a-synuclein oligomerization and nitration: intermediacy of carbonate radical anion and nitrogen dioxide radical, Biochem. J. 378, 435-447.
123. Berlett, B. S., Chock, P. B., Yim, M. B., and Stadtman, E. R. (1990) Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid-facilitated dismutation of hydrogen peroxide, Proc. Natl. Acad. Sci. USA 87, 389-393.
124. Gomazkova, V. S. (1973) Effect of thiamine pyrophosphate and of the ions of divalent metals on the activity and stability of the a-ketoglutarate decarboxylase from the breast muscle of the pigeon [Russian], Biokhimiia 38, 756-762.
125. Markiewicz, J., and Strumilo, S. (1997) The effect of Mn2{thorn} on the catalytic function of heart muscle 2-oxoglutarate dehydrogenase complex, Biochem. Arch. 13, 127-129.
126. Bunik, V., Westphal, A. H., and de Kok, A. (2000) Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate, Eur. J. Biochem. 267, 3583-3591.