Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen

FEBS Letters

Volumn 580, Issue 17, 2006, Pages 4069-4072

  Ueki, Yusaku ^a   Inoue, Megumi ^a   Kurose, Shinji ^a   Kataoka, Kunishige ^a   Sakurai, Takeshi ^a  

^a KANAZAWA UNIVERSITY   (Japan)

Author keywords

CueO; Four electron reduction of dioxygen; Multicopper oxidase; Point mutation; Trinuclear Cu center

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; COPPER; GLUTAMINE; HYDROGEN; OXIDOREDUCTASE; OXYGEN; PROTON; WATER;

ARTICLE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; OXYGEN AFFINITY; POINT MUTATION; PRIORITY JOURNAL; REDUCTION; SPECTROSCOPY;

ASPARTIC ACID; BINDING SITES; CIRCULAR DICHROISM; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI PROTEINS; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN;

EID: 33745870084     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.06.049     Document Type: Article

References (16)

1. Messerschmidt A., Ladenstein R., Huber R., Bolognesi M., Avigliano L., Petruzzelli R., Rossi, and Finazzi-Agro A. Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J. Mol. Biol. 224 (1992) 179-205
2. Zaitseva I., Zairsev V., Card G., Moshkov K., Bax B., Ralph A., and Lindley P. The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centers. J. Biol. Inorg. Chem. 1 (1996) 15-23
3. Piontek K., Antorini M., and Choinowski T. Crystal structure of a laccase from the fungus Trametes versicolor at 1.9 Å resolution containing a full component of coppers. J. Biol. Chem. 40 (2002) 37663-37669
4. Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., and Rouvinen J. Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nat. Struct. Biol. 9 (2002) 601-605
5. Bertland T., Jolivalt C., Briozzo P., Caminade E., Joly N., Madzak C., and Mougin C. Crystal structure of a four-copper laccase complexes with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41 (2002) 7325-7333
6. Enguita F.J., Martins L.O., Henriques A.O., and Carrondo M.A. Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties. J. Biol. Chem. 278 (2003) 19416-19425
7. Roberts W.A., Weichsel A., Grass G., Yhakali K., Hazzard J.T., Tollin G., Rensing C., and 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 99 (2002) 2766-2771
8. Taylor A.B., Stoj C.S., Ziegler L., Kosman D.J., and Hart P.J. The copper-iron connection in biology: structure of the metallo-oxidase Fet3p. Proc. Natl. Acad. Sci. USA 102 (2005) 15459-15464
9. Huang H., Zoppellaro G., and Sakurai T. Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase. J. Boil. Chem. 274 (1999) 32718-32724
10. Zoppellaro G., Sakurai T., and Huang H. A novel mixed valence form of Rhus vernicifera laccase and its reaction with dioxygen to give a peroxide intermediate bound to the trinuclear center. J. Biochem. 129 (2001) 949-953
11. Palmer A.E., Lee S.K., and Solomon E.I. Decay of the peroxide intermediate in laccase: reductive cleavage of the O-O bond. J. Am. Chem. Soc. 123 (2001) 6591-6599
12. 2O at the trinuclear cluster active site in native laccase. J. Am. Chem. Soc. 124 (2002) 6180-6193
13. Quintanar L., Stoj C., Wang T.-P., Kosman D.J., and Solomon E.I. Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p. Biochemistry 44 (2005) 6081-6091
14. Kataoka K., Kitagawa R., Inoue M., Naruse D., Sakurai T., and Huang H. Point mutations at the type I Cu ligands, Cys457 and Met467, and at the putative proton donor, Asp105, in Myrothecium verrucaria bilirubin oxidase and reactions with dioxygen. Biochemistry 44 (2005) 7004-7012
15. Roberts S.A., Wildner G.F., Grass G., Weichsel A., Ambrus A., Rensing C., and Montford W.R. A labile regulatory copper ions near the T1 copper site in the multicopper oxidase CueO. J. Biol. Chem. 278 (2003) 31958-31963
16. Shimizu A., Kwon J.-H., Sasaki T., Satoh T., Sakurai N., Sakurai T., Yamaguchi S., and Samejima T. Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands. Biochemistry 38 (1999) 3034-3042