Ascaris suum NADH-methemo(myo)globin reductase systems recovering differential functions of hemoglobin and myoglobin, adapting to environmental hypoxia

Parasitology International

Volumn 58, Issue 3, 2009, Pages 278-284

  Takamiya, Shinzaburo ^a   Hashimoto, Muneaki ^a   Kazuno, Saiko ^a   Kikkawa, Mika ^a   Yamakura, Fumiyuki ^b  

^a JUNTENDO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b JUNTENDO UNIVERSITY   (Japan)

Author keywords

Ascaris suum; Cytochrome b5; Hypoxia; NADH methemo(myo)globin reductase

Indexed keywords

CYTOCHROME B5; HEMOGLOBIN; METHEMOGLOBIN; METHEMOGLOBIN REDUCTASE; METMYOGLOBIN; MYOGLOBIN; OXYGEN;

ARTICLE; ASCARIS SUUM; HOMEOSTASIS; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION;

ADAPTATION, PHYSIOLOGICAL; ANIMALS; ANOXIA; ASCARIS SUUM; CYTOCHROME-B(5) REDUCTASE; CYTOCHROMES B5; HEAT-SHOCK RESPONSE; HELMINTH PROTEINS; HEMOGLOBINS; MYOGLOBIN; OXIDOREDUCTASES; OXYGEN;

ASCARIS; ASCARIS SUUM; MAMMALIA;

EID: 67650435867     PISSN: 13835769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.parint.2009.03.003     Document Type: Article

References (28)

1. Komuniecki P.R., and Vanover L. Biochemical changes during the aerobic-anaerobic transition in Ascaris suum larvae. Mol Biochem Parasitol 22 (1987) 241-248
2. Vanover-Dettling L., and Komuniecki P.R. Effects of gas phase on carbohydrate metabolism in Ascaris suum larvae. Mol Biochem Parasitol 36 (1989) 29-40
3. Takamiya S., Kita K., Wang H., Weinstein P.P., Hiraishi A., Oya H., et al. Developmental changes in the respiratory chain of Ascaris mitochondria. Biochim Biophys Acta 1141 (1993) 65-74
4. Mei B., Komuniecki P.R., and Komuniecki R. Localization of cytochrome oxidase and the 2-methyl branched-chain enoyl CoA reductase in muscle and hypodermis of Ascaris suum larvae and adults. J Parasitol 83 (1997) 760-763
5. Komuniecki R., and Komuniecki P.R. Aerobic-anaerobic transitions during the development of the parasitic nematode, Ascaris suum. In: Boothroyd J.C., and Komuniecki R. (Eds). Molecular approaches to parasitology (1995), Wiley-Liss, New York 109-121
6. Kita K., and Takamiya S. Electron-transfer complexes in Ascaris mitochondria. Adv Parasitol 51 (2002) 95-131
7. Amino H., Osanai A., Miyadera H., Shinjyo N., Tomitsuka E., Taka H., et al. Isolation and characterization of the stage-specific cytochrome b small subunit (CybS) of Ascaris suum complex II from the aerobic respiratory chain of larval mitochondria. Mol Biochem Parasitol 128 (2003) 175-186
8. Iwata F., Shinjyo N., Amino H., Sakamoto K., Khyrul Islam M., Tsuji N., et al. Change of subunit composition of mitochondrial complex II (succinate-ubiquinone reductase/quinol-fumarate reductase) in Ascaris suum during the migration in the experimental host. Parasitol Int 57 (2008) 54-61
9. Behm C.A. Chapter10 metabolism. In: Lee L. (Ed). The biology of nematodes (2002), Taylor and Francis, New York 261-291
10. Blaxter M.L. Nemoglobins: divergent nematode globins. Parasitol Today 9 (1993) 353-360
11. Goldberg D.E. The enigmatic oxygen-avid hemoglobin of Ascaris. BioEssays 17 (1995) 177-182
12. Barrett J., and Brophy P.M. Ascaris haemoglobin: new tricks for an old protein. Parasitol Today 16 (2000) 90-91
13. 5-type cytochrome: an additional α-helix and positively charged residues on the surface domain interact with redox partners. Biochem J 394 (2006) 437-447
14. 5, an adult-specific secretory protein reducing oxygen-avid ferric hemoglobin. Archiv Biochem Biophys 471 (2008) 42-49
15. Okazaki T., Wittenberg B.A., Briehl R.W., and Wittenberg J.B. The hemoglobin of Ascaris body walls. Biochim Biophys Acta 140 (1967) 258-265
16. Wittenberg B.A., Okazaki T., and Wittenberg J.B. The hemoglobin of Ascaris perienteric fluid. I. Purification and spectra. Biochim Biophys Acta 111 (1965) 485-495
17. 5 precursor protein: a histidine-tagged full-length presequence is correctly processed to transport the mature protein to the periplasm of Escherichia coli. Arch Biochem Biophys 413 (2003) 253-261
18. Dutton P.L. Redox potentiometry: determination of midpoint potentials of oxidation and reduction components of biological electron-transfer systems. Methods Enzymol 54 (1978) 411-435
19. O'Reilly J.E. Oxidation-reduction potential of the ferro-ferricyanide system in buffer solutions. Biochem Biophys Acta 292 (1973) 509-515
20. Taboy C.H., Bonaventura C., and Crumbliss A.L. Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry. Methods Enzymol 353 (2002) 187-209
21. Di Iorio E.E. Preparation of derivatives of ferrous and ferric hemoglobin. Methods Enzymol 76 (1981) 57-72
22. Darawshe S., Tsafadyah Y., and Daniel E. Quaternary structure of erythrocruorin from the nematode Ascaris suum: evidence for unsaturated haem-binding sites. Biochem J 242 (1987) 689-694
23. Wittenberg J.B. Facilitated oxygen diffusion: the role of leghemoglobin in nitrogen fixation by bacteroides isolated from soybean root nodules. J Biol Chem 249 (1974) 4057-4066
24. Blaxter M.L., Vanfeteren J.R., Xia J., and Moens L. Structural characterization of an Ascaris myoglobin. J Biol Chem 269 (1994) 30181-30186
25. Blair K.L., Barsuhn C.L., Day J.S., Ho N.F.H., Geary T.G., and Thompson D.P. Biophysical model for organic acid excretion in Ascaris suum. Mol Biochem Parasitol 93 (1998) 179-190
26. 5 and human methemoglobin. Biochemistry 21 (1982) 4730-4734
27. 5. J Biol Inorg Chem 7 (2002) 580-588
28. Weber R.E. Functions of invertebrate hemoglobins with special reference to adaptations to environmental hypoxia. Amer Zool 20 (1980) 79-101