ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase

FEBS Letters

Volumn 584, Issue 18, 2010, Pages 4027-4031

  Iwaki, Masayo ^a   Kataoka, Kunishige ^b   Kajino, Tsutomu ^a   Sugiyama, Ryosuke ^b   Morishita, Hirotoshi ^b   Sakurai, Takeshi ^b  

^a Rd Management Section   (Japan)

^b KANAZAWA UNIVERSITY   (Japan)

Author keywords

Attenuated total reflectance Fourier transform infrared; Bilirubin oxidase; CueO; Multicopper oxidase; Oxygen reduction; Proton transfer

Indexed keywords

AMINO ACID; BILIRUBIN OXIDASE; CARBOXYLIC ACID; GLUTAMIC ACID; GLUTAMINE; MULTICOPPER OXIDASE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; CUEO PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; PROTON;

ARTICLE; CATALYSIS; CONTROLLED STUDY; COPPER METABOLISM; ELECTROCHEMISTRY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME METABOLISM; ENZYME PURIFICATION; FUNGUS; INFRARED SPECTROSCOPY; MUTAGENESIS; MYROTHECIUM VERRUCARIA; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; REFLECTOMETRY; WILD TYPE; CHEMISTRY; GENETICS; MUTATION;

ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; GLUTAMINE; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTONS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 77956928109     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.08.018     Document Type: Article

References (23)

1. Grass G., Rensing C. Genes involved in copper homeostasis in Escherichia coli. J. Bacteriol. 2001, 183:2145-2147.
2. Roberts S.A., Weichsel A., Grass G., Thakali K., Hazzard J.T., Tollin G., Rensing C., Montfort W.R. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. USA 2002, 99:2766-2771.
3. Sakurai T., Kataoka K. Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. Chem. Rec. 2007, 7:220-229.
4. Koikeda S., Ando K., Kaji H., Inoue T., Murao S., Takeuchi K., Samejima T. Molecular cloning of the gene for bilirubin oxidase from Myrothecium verrucaria and its expression in yeast. J. Biol. Chem. 1993, 268:18801-18809.
5. Enguita F.J., Martins L.O., Henriques A.O., Carrondo M.A. Crystal structure of a bacterial endospore coat component: a laccase with enhanced thermostability properties. J. Biol. Chem. 2003, 278:19416-19425.
6. Messerschmidt A., Ladenstein R., Huber R., Bolognesi M., Avigliano L., Petruzzelli R., Rossi A., Finazzi-Agró A. Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J. Mol. Biol. 1992, 224:179-205.
7. Taylor A.B., Stoj C.S., Ziegler L., Kosman D.J., Hart P.J. The copper-iron connection in biology: structure of the metallo-oxidase Fet3p. Proc. Natl. Acad. Sci. USA 2005, 102:15459-15464.
8. Bertland T., Jolivalt C., Briozzo P., Caminade E., Joly N., Madzak C., Mougin C. Crystal structure of a four-copper laccase complexes with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 2002, 41:7325-7333.
9. Hakulinen N., Andbergb M., Kallioa J., Koivulab A., Kruusb K., Rouvinena J. A near atomic resolution structure of a Melanocarpus albomyces laccase. J. Struct. Biol. 2008, 162:29-39.
10. 506 located adjacent to the trinuclear copper center. J. Biol. Chem. 2009, 284:14405-14413.
11. Augustine A.J., Quintanar L., Stoj C.S., Kosman D.J., Solomon E.I. Spectroscopic and kinetic studies of perturbed trinuclear copper clusters: the role of protons in reductive cleavage of the O-O bond in the multicopper oxidase Fet3p. J. Am. Chem. Soc. 2007, 129:13118-13126.
12. Chen Z., Durão P., Silva C.S., Pereira M.M., Todorovic S., Hildebrandt P., Bento I., Lindley P.F., Martins L.O. The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis. Dalton Trans. 2010, 39:2875-2882.
13. Mizutani K., Toyoda M., Sagara K., Takahashi N., Sato A., Kamitaka Y., Tsujimura S., Nakanishi Y., Sugiura T., Yamaguchi S., Kano K., Mikami B. X-ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 Å resolution using a twinned crystal. Acta Crystallogr. 2010, F66:765-770.
14. Kataoka K., Tanaka K., Sakai Y., Sakurai T. High-level expression of Myrothecium verrucaria bilirubin oxidase in Pichia pastoris, and its facile purification and characterization. Protein Expr. Purif. 2005, 41:77-83.
15. Glasoe P.K., Long F.A. Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 1960, 64:188-190.
16. Marshall D., Fisher N., Grigic L., Zickermann V., Brandt U., Shannon R.J., Hirst J., Lawrence R., Rich P.R. ATR-FTIR redox difference spectroscopy of Yarrowia lipolytica and bovine complex I. Biochemistry 2006, 45:5458-5467.
17. Rich P.R., Iwaki M. Methods to probe protein transitions with ATR infrared spectroscopy. Mol. Biosyst. 2007, 3:398-407.
18. Miura Y., Tsujimura S., Kurose S., Kamitaka Y., Kataoka K., Sakurai T., Kano K. Direct electrochemistry of CueO and its mutants at residues to and near type I Cu for oxygen-reducing biocathode. Fuel Cells 2009, 9:70-78.
19. Tsujimura S., Kuriyama A., Fujieda N., Kano K., Ikeda T. Mediated spectroelectrochemical titration of proteins for redox potential measurements by a separator-less one-compartment bulk electrolysis method. Anal. Biochem. 2005, 337:325-331.
20. Ueki Y., Inoue M., Kurose S., Kataoka K., Sakurai T. Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen. FEBS Lett. 2006, 580:4069-4072.
21. I) poplar plastocyanin at six pH values. J. Mol. Biol. 1986, 192:361-387.
22. Bagby S., Driscoll P.C., Harvey T.S., Hill H.A.O. High-resolution solution structure of reduced parsley plastocyanin. Biochemistry 1994, 33:6611-6622.
23. Taneva S.G., Kaiser U., Donchev A.A., Dimitrov M.I., Mäntele W., Muga A. Redox-induced conformational changes in plastocyanin: an infrared study. Biochemistry 1999, 38:9640-9647.