A H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis

European Journal of Biochemistry

Volumn 241, Issue 1, 1996, Pages 155-161

  Brown, David M ^a   Upcroft, Jacqueline A ^a   Upcroft, Peter ^a  

^a QIMR BERGHOFER MEDICAL RESEARCH INSTITUTE   (Australia)

Author keywords

Drug reduction; Flavoenzyme; Giardia duodenalis; NADH oxidase; Water producing

Indexed keywords

FURAZOLIDONE; METRONIDAZOLE; NITROFURANTOIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; AMINO ACID; ENZYME INHIBITOR; MULTIENZYME COMPLEX; OXIDOREDUCTASE; WATER;

ARTICLE; DRUG TRANSFORMATION; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; GEL ELECTROPHORESIS; GIARDIA; IN VITRO STUDY; MITOCHONDRIAL RESPIRATION; MOLECULAR WEIGHT; PRIORITY JOURNAL; SEQUENCE ANALYSIS; AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ANIMAL; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY;

GIARDIA; GIARDIA INTESTINALIS; PROTOZOA;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CHROMATOGRAPHY, AFFINITY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; GIARDIA; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MULTIENZYME COMPLEXES; NADH, NADPH OXIDOREDUCTASES; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SPECTROPHOTOMETRY; WATER;

EID: 0029661970     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0155t.x     Document Type: Article

References (51)

1. Ahmed, S. A. & Claiborne, A. (1989) The streptococcal flavoprotein NADH oxidase, J. Biol. Chem. 264, 19856-19863.
2. Blusson, H., Petitdemange, H. & Gay, R. (1981) A new, fast, and sensitive assay for NADH-ferredoxin oxidoreductase detection in clostridia, Anal. Biochem. 110, 176-181.
3. Boreham, P. F. L., Phillips, R. E. & Shepherd. R. W. (1986) The activity of drugs against Giardia intestinalis in neonatal mice, J. Antimicrob. Chemother. 18, 393-398.
4. Bradford, M. M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 72, 248-254.
5. Brown, D. M., Upcroft, J. A. & Upcroft, P. (1993) Cysteine is the major low molecular mass thiol in Giardia duodenalis, Mol. Biochem. Parasitol. 61, 155-158.
6. Brown, D. M., Upcroft, J. A. & Upcroft, P. (1995) Free radical detoxification in Giardia duodenalis, Mol. Biochem. Parasitol. 72, 47-56.
7. Cavalier-Smith, T. (1987) The origin of eukaryote and archaebacterial cells, Endocytobiology III, Ann. N. Y. Acad, Sci. 503, 17-54.
8. Cavalier-Smith, T. (1993) Kingdom Protozoa and its 18 phyla, Microbiol. Rev. 57, 953-994.
9. Chen, J.-S. & Blanchard, D. K. (1979) A simple hydrogenase-linked assay for ferredoxin and flavodoxin, Anal. Biochem. 93, 216-222.
10. Cocco, D., Rinaldi, A., Savini, Cooper, J. M. & Bannister, J. V. (1988) NADH oxidase from the extreme thermophile Thermus aquanticus YT-1. Purification and characterisation, Eur. J. Biochem. 174, 269-280.
11. Davies, G. E. & Stark, G. R. (1970) Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins, Proc. Natl Acad. Sci. USA 66, 651-656.
12. Decker, L. A. (ed.) (1977) Worthington enzyme manual, Worthington Biochemical Corp., Freehold NJ.
13. Edwards, M. R., Schofield, P. J., O'Sullivan, W. J. & Costello, M. (1992) Arginine metabolism during culture of Giardia intestinalis, Mol. Biochem. Parasitol. 53, 97 - 104.
14. Ellis, J. E., Cole, D. & Lloyd, D. (1992) Influence of oxygen on the fermentative metabolism of metronidazole-sensitive and resistant strains of Trichomonas vaginalis, Mol. Biochem. Parasitol. 56, 79 - 88.
15. Faeder, E. J. & Siegel, L. M. (1973) A rapid micromethod for determination of FMN and FAD in mixtures. Anal. Biochem. 53. 332 - 336.
16. Gomori, G. (1955) Preparation of buffers for use in enzyme studies, Methods Enzymol. I. 138 - 146.
17. Greer, S. & Perham, R. N. (1986) Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene relationship to other flavoprotein disulphide oxidoreductases, Biochemistry 25, 2736-2742.
18. Hatefi, Y. (1985) The mitochondrial electron transport and oxidative phosphorylation system, Annu. Rev. Biochem. 54, 1015 - 1069.
19. Healey, A., Mitchell, R., Upcroft, J. A., Boreham, P. F. L. & Upcroft. P. (1990) Complete nucleotide sequence of the ribosomal RNA tandem repeat unit from Giardia instestinalis, Nucleic Acids Res. 18, 4006.
20. Hoskins, D. D., Whiteley, H. R. & Mackler, B. (1962) The reduced diphosphopyridine nucleotide oxidase of Streptococcus faecalis: purification and properties, J. Biol. Chem. 237, 2647 - 2651.
21. Hunt, J. & Massey, V. (1992) Purification and properties of milk xanthine dehydrogenase. J. Biol. Chem. 267, 21479 - 21485.
22. Karplus, P. A. & Schulz, G. E. (1987) Refined structure of glutathione reductase at 1. 5 Å resolution, J. Mol. Biol. 195, 701 - 729.
23. Klömkes, M., Altdorf, R. & Ohlenbusch, H.-D. (1985) Purification and properties of an FAD-containing NADH oxidase from Mycoplasma capricolum, Biol. Chem. Hoppe-Seyler 366, 963 - 969.
24. Koike, K., Kobayashi, Ito, S. & Saitoh, M. (1985) Purification and characterization of NADH oxidase from a strain of Leuconostoc mesenteroides, J. Biochem. (Tokyo) 97, 1279 - 1288.
25. Laemmli, U. K. (1970) Cleavage of the structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680 - 685.
26. Lindmark, D. G. (1980) Energy metabolism of the anaerobic protozoan Giardia lamblia, Mol. Biochem. Parasitol. 1, 1-12.
27. Linstead, D. J. & Bradley, S. (1988) The purification and properties of two soluble reduced nicotinamide: acceptor oxidoreductases from Trichomonas vaginalis, Mol. Biochem. Parasitol. 27, 125 - 134.
28. Lo, H.-S. & Reeves, R. E. (1980) Purification and properties of NADPH: flavin oxidoreductase from Entamoeba histolytica, mol. Biochem. Parasitol. 2, 23 - 30.
29. Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951) Protein measurement with the folin phenol reagent, J. Biol. Chem. 193, 265 - 275.
30. Maeda, K., Truscott, K., Liu X. L. & Scopes, R. K. (1992) A thermostable NADH oxidase from anaerobic extreme thermophiles, Biochem. J. 284, 551 - 555.
31. Mertens, E. (1993) ATP versus pyrophosphate: glycolysis revisited in parasitic protists, Parasitol. Today 9, 122 - 126.
32. Moreno, S. N. J., Mason, R. P. & Docampo, R. (1984) Distinct reduction of nitrofurans and metronidazole to free radical metabolites by Tritrichomonas foetus hydrogenosomal and cytosolic enzymes, J. Biol. Chem. 259, 8252 - 8259.
33. Ohnishi, K., Niimura, Y., Yokoyama, K., Hidaka, M., Masaki, H., Uchimura, T., Suzuki, H., Uozumi, T., Kozaki, M., Komagata, K. & Nishino, T. (1994) Purification and analysis of a flavoprotein functional as NADH oxidase from Amphibacillus xylanus overexpressed in Escherichia coli, J. Biol. Chem. 269, 31418 - 31423.
34. Paget, T. A., Lloyd, D., Jarroll, E. L., Manning, P. & Lindmark, D. G. (1989) Respiratory activity in Giardia spp., in Biochemistry and molecular biology of anaerobic protozoa (Lloyd, D., Coombs, G. H. and Paget, T. A., eds) pp. 186 - 201, Harwood Academic Publishers GmbH, Reading UK.
35. Park, H.-J., Reiser, C. O. A., Kondruweit, S., Erdmann, H., Schmidt, R. D. & Sprinzl, M. (1992) Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8. Eur. J. Biochem. 205, 881 - 885.
36. Poole, L. B. & Claiborne, A. (1989) The non-flavin redox centre of the streptococcal NADH peroxidase. II. Evidence for a stabilised cysteine-sulfenic acid, J. Biol. Cliem. 264, 12322 - 12329.
37. Reinards, R., Kubicki, J. & Ohlenbusch, H.-D. (1981) Purification and characterisation of NADH oxidise from membranes of Acholeplasma laidlaii, a copper-containing iron-sulfur flavoprotein. Eur. J. Biochem. 120, 329 - 337.
38. Ross, R. P. & Claiborne, A. (1992) Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10CI : comparison with NADH peroxidase and the flavoprotein disulfide reductases, J. Mol. Biol. 227, 658 - 671.
39. Russel, M. & Model, P. (1988) Sequence of thioredoxin reduciase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases, J. Biol. Chem. 263, 9015 - 9019.
40. Saeki, Y., Nozaki, M. & Matsumoto, K. (1985) Purification and properties of NADH oxidase from Bacillus megaterium. J. Biochem. (Tokyo) 98, 1433 - 1440.
41. 2O-forming NADH oxidase from Streptococcus faecalis, Eur. J. Biochem. 156, 149 - 155.
42. Sogin, M. L., Gunderson, J. H., Elwood, H. J., Alonso, R. A. &. Peattie, D. A. (1989) Phylogenetic meaning of the kingdom concept: an unusual ribosomal RNA from Giardia lamblia, Science 243, 75 - 77.
43. Stanton, T. B. & Jensen, N. S. (1993) Purification and characterization of NADH oxidase from Serpulina (Treponema) hyodysenteriae, J. Bacteriol. 175, 2980 - 2987.
44. Townson, S. M., Laqua, H., Upcroft, P., Boreham, P. F. L. & Upcroft, J. A. (1992) Induction of metronidazole and furazolidone resistance in Giardia, Trans. R. Soc. Trop. Med. Hyg. 86, 521 - 522.
45. Townson, S. M., Hanson, G. R., Upcroft, J. A. & Upcroft, P. (1994a) A purified ferredoxin from Giardia duodenalis, Eur. J. Biochem. 220, 439-446.
46. Townson, S. M., Boreham, P. F. L., Upcroft, P. &. Upcroft, J. A. (1994b) Resistance to the nitroheterocyclic drugs, Acta Tropica 56, 173 - 194.
47. Townson, S. M., Upcroft, J. A. & Upcroft, P. (1996) Characterisation and purification of pyruvate: ferredoxin oxidoreductase from Giardia duodenalis, Mol. Biochem. Parasitol. 19, 183 - 193.
48. Upcroft, J. A., Healey, A., Mitchell, R., Boreham, P. F. L. & Upcroft, P. (1990). Antigen expression from the ribosomal repeat of Giardia intestinalis, Nucleic Acids Res. 18. 7077-8081.
49. Upcroft. J. A. & Upcroft, P. (1993) Drug resistance and Giardia, Parasitol. Today 9, 187-190.
50. Weinbach, E. C., Claggett, E., Keister, D. B., Diamond, L. S. & Kon, H. (1980) Respiratory metabolism of Giardia lamblia, J. Parasitol. 66, 347-350.
51. Wierenga, R. K., Terpstra, P. & Hol, W. G. J. (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107.