Indolepyruvate ferredoxin oxidoreductase: An oxygen-sensitive iron-sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus

Journal of Bioscience and Bioengineering

Volumn 114, Issue 1, 2012, Pages 23-27

  Ozawa, Yukiko ^a   Siddiqui, Masood Ahmed ^a,d   Takahashi, Yasufumi ^a   Urushiyama, Akio ^a   Ohmori, Daijiro ^b   Yamakura, Fumiyuki ^b   Arisaka, Fumio ^c   Imai, Takeo ^a  

^a RIKKYO UNIVERSITY   (Japan)

^b JUNTENDO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^d UNIVERSITY OF BALOCHISTAN   (Pakistan)

Author keywords

Ferredoxin; Hyperthermophile; Indolepyruvate; Oxidoreductase; Oxygen sensitive; Thermococcus

Indexed keywords

FERREDOXIN; HYPERTHERMOPHILES; INDOLEPYRUVATE; OXIDOREDUCTASES; OXYGEN-SENSITIVE; THERMOCOCCUS;

FERMENTATION; MICROORGANISMS; OXYGEN; PEPTIDES; SULFUR;

ENZYMES;

BACTERIAL ENZYME; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE; OXYGEN; PYRUVATE SYNTHASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; HALF LIFE TIME; HIGH TEMPERATURE; HYPERTHERMOPHILIC ARCHAEON; NONHUMAN; OXYGEN SENSING; THERMOCOCCUS; THERMOCOCCUS PROFUNDUS; WATER TEMPERATURE;

ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME ACTIVATION; ENZYME INHIBITORS; ENZYME STABILITY; HALF-LIFE; HOT TEMPERATURE; IRON; KETONE OXIDOREDUCTASES; MOLECULAR WEIGHT; OXYGEN; SULFUR; THERMOCOCCUS;

ARCHAEA; THERMOCOCCUS; THERMOCOCCUS PROFUNDUS;

EID: 84862766096     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.02.014     Document Type: Article

References (30)

1. Adams M.W.W. Enzyme and proteins from organisms that grow near and above 100°C. Ann. Rev. Microbiol. 1993, 47:627-658.
2. Adams M.W.W. Biochemical diversity among sulfur-dependent hyperthermophilic microorganism. FEMS Microbiol. Rev. 1994, 15:267-277.
3. Adams M.W.W., Park J.-B., Mukund S., Blamey J., Kelly R.M. Biocatalysis at extreme temperature: Enzyme system near and above 100°C 1992, vol. 498. Metabolic enzymes from sulfur-dependent, extremely thermophilic organisms, p. 4-22, American Chemical Society, Washington, D.C. M.W.W. Adams, R.M. Kelly (Eds.).
4. Ma K., Loessner H.J., Heider J., Johnson M.K., Adams M.W.W. Effect of elemental sulfur on the metabolism of the deep-sea hyperthermophilic archaeon Thermococcus strain ES-1: characterization of a sulfur-regulated, non-heme iron alcohol dehydrogenase. J. Bacteriol. 1995, 177:4748-4756.
5. Heider J., Ma K., Adams M.W.W. Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1. J. Bacteriol. 1995, 177:4757-4764.
6. Matsumi R., Atomi H., Imanaka T. Biochemical properties of a putative signal peptide peptidase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 2005, 187:7072-7080.
7. Morikawa M., Izawa Y., Rashid N., Hoaki T., Imanaka T. Purification and characterization of thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp. Appl. Environ. Microbiol. 1994, 60:4559-4566.
8. Schafer T., Selig M., Schonheit P. Acetyl CoA synthetase (ADP-forming) in archaea, a novel enzyme involved in acetate formation and ATP synthesis. Arch. Microbiol. 1993, 159:72-83.
9. Schut J., Menon A.L., Adams M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 2001, 331:144-158.
10. Blamey J.M., Adams M.W.W. Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. Biochim. Biophys. Acta 1993, 1161:19-27.
11. Blamey J.M., Adams M.W.W. Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium Thermotoga maritima. Biochemistry 1994, 33:1000-1007.
12. Mai X., Adams M.W.W. Indolepyruvate ferredoxin oxidoreductase from a hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 1994, 269:16726-16732.
13. Kletzin A., Adams M.W.W. Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductase from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima. J. Bacteriol. 1996, 178:248-257.
14. Heider J., Mai X., Adams M.W.W. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J. Bacteriol. 1996, 178:780-787.
15. Mai X., Adams M.W.W. Characterization of a four type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J. Bacteriol. 1996, 178:5890-5896.
16. Siddiqui M.A., Fujiwara S., Imanaka T. Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1 possesses a mosaic structure showing features of various oxidoreductases. Mol. Gen. Genet. 1997, 254:433-439.
17. Ozawa Y., Nakamura T., Kamata N., Yasujima D., Urushiyama A., Yamakura F., Ohmori D., Imai T. Thermococcus profundus 2-ketoisovalerate ferredoxin oxidoreductase, a key enzyme in the archaeal energy-producing amino acid metabolic pathway. J. Biochem. 2005, 137:101-107.
18. Chabriere E., Charon M.-H., Volbeda A., Pieulle L., Hatchikian E.C., Fontecilla-Campus J.-C. Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate. Nat. Struct. Biol. 1999, 6:182-190.
19. Siddiqui M.A., Fujiwara S., Takagi M., Imanaka T. In vitro heat effect on heterooligomeric subunit assembly of thermostable indolepyruvate ferredoxin oxidoreductase. FEBS Lett. 1998, 434:372-376.
20. Siddiqui M.A., Fujiwara S., Takagi M., Imanaka T. Phylogenetic analysis and effect of heat on conformational change of ferredoxin from hyperthermophilic archaeon Pyrococcus sp. KOD1. J. Ferment. Bioeng. 1998, 85:271-277.
21. Kobayashi T., Kwak Y.S., Akiba T., Kudo T., Horikoshi K. Thermococcus profundus sp. nov., a new hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent system. Appl. Microbiol. 1994, 17:232-236.
22. Davis B.J. Disc electrophoresis-II. Method and application to human serum proteins. Ann. N.Y. Sci. 1964, 121:404-427.
23. Weber K., Osborn M. The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 1969, 244:4406-4412.
24. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
25. Imai T., Yasujima D., Siddiqui M.A. An instant measurement of oxidoreductase activity above 100°C by monitoring the absorbance change. J. Biosci. Bioeng. 2004, 97:336-338.
26. Robb F.T., Maeder D.L., Brown J.R., DiRuggiero J., Stump M.D., Yeh R.K., Weiss R.B., Dunn D.M. Genomic sequence of hyperthermophile. Pyrococcus furiosus: implications for physiology and enzymology. Methods Enzymol. 2001, 330:134-157.
27. Imai T., Saito H., Tobari J., Ohmori D., Suzuki K. Resonance Raman spectroscopic evidence for the presence of 4Fe and 3Fe centers in Pseudomonas ovalis ferredoxin and Mycobacterium smegmatis ferredoxin. FEBS Lett. 1984, 165:227-230.
28. Imai T., Matsumoto T., Ohta S., Ohmori D., Suzuki K., Tanaka J., Tsukioka M., Tobari J. Isolation and characterization of a ferredoxin from Mycobacterium. Biochim. Biophys. Acta 1983, 743:91-97.
29. Johnson M.K., Spiro T.G., Mortenson L.E. Resonance Raman and electron paramagnetic resonance studies on oxidized and ferricyanide-treated Clostridium pasteurianum ferredoxin. Vibrational assignments from 34S shifts and evidence for conversion of 4 to 3 iron-sulfur clusters via oxidative damage. J. Biol. Chem. 1982, 257:2447-2452.
30. Johnson M.K., Czernuszewicz R.S., Spiro T.G., Fee J.A., Sweeney W.V. Resonance Raman spectroscopic evidence for a common [3Fe-4S] structure among proteins containing three-iron centers. J. Am. Chem. Soc. 1983, 105:6671-6678.