Identification of a radical intermediate in the enzymatic reduction of oxygen by a small laccase

Journal of the American Chemical Society

Volumn 131, Issue 33, 2009, Pages 11680-11682

  Tepper, Armand W J W ^a   Milikisyants, Sergey ^b   Sottini, Silvia ^b   Vijgenboom, Erik ^a   Groenen, Edgar J J ^b   Canters, Gerard W ^a,b  

^a LEIDEN UNIVERSITY   (Netherlands)

^b LEIDEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL EQUATIONS; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; ENZYMATIC REDUCTION; ENZYME MECHANISM; LACCASES; OPTICAL CHARACTERISTICS; SPIN-SPIN; STREPTOMYCES COELICOLOR; TYROSYL RADICALS;

CHEMICAL REACTIONS; ENZYMES; LIGHT TRANSMISSION; MOLECULAR OXYGEN; PARAMAGNETIC RESONANCE; PARAMAGNETISM; SPECTROSCOPY; SPIN DYNAMICS;

ELECTRON SPIN RESONANCE SPECTROSCOPY;

ASCORBATE OXIDASE; CUPRIC ION; LACCASE; OXYGEN;

ARTICLE; ELECTRON SPIN RESONANCE; ENZYME KINETICS; ENZYME MECHANISM; REDUCTION;

ABSORPTION; CATALYTIC DOMAIN; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICALS; LACCASE; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXYGEN; SORDARIALES; SPECTRUM ANALYSIS;

EID: 69049089802     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja900751c     Document Type: Article

References (20)

1. Machczynski, M. C.; Vijgenboom, E.; Samyn, B.; Canters, G. W. Protein Sci. 2004, 13, 2388.
2. Messerschmidt, A.; Ladenstein, R.; Huber, R.; Bolognesi, M.; Avigliano, L.; Petruzzelli, R.; Rossi, A.; Finazziagro, A. J. Mol. Biol. 1992, 224, 179.
3. Messerschmidt, A. Multi-Copper Oxidases; World Scientific Publishing: Singapore, 1997.
4. Solomon, E. I.; Augustine, A. J.; Yoon, J. Dalton Trans. 2008, 3921.
5. Aasa, R.; Branden, R.; Deinum, J.; Malmstrom, B. G.; Reinhammar, B.; Vanngard, T. FEBS Lett. 1976, 61, 115.
6. Andreasson, L. E.; Branden, R.; Reinhammar, B. Biochim. Biophys. Acta 1976, 438, 370.
7. Solomon, E. I.; Chen, P.; Metz, M.; Lee, S. K.; Palmer, A. E. Angew. Chem., Int. Ed. 2001, 40, 4570.
8. Morie-Bebel, M. M.; McMillin, D. R.; Antholine, W. E. Biochem. J. 1986, 235, 415.
9. Cole, J. L.; Ballou, D. P.; Solomon, E. I. J. Am. Chem. Soc. 1991, 113, 8544.
10. The small difference is primarily due to the different circumstances under which the optical and EPR samples had to be prepared and studied. In particular, the time scale of the reaction in the EPR experiment is less well defined because of the freeze - thaw cycles involved.
11. Eaton, S. S.; More, K. M.; Sawant, B. M.; Eaton, G. R. J. Am. Chem. Soc. 1983, 105, 6560.
12. Michel, F.; Thomas, F.; Hamman, S.; Philouze, C.; Saint-Aman, E.; Pierre, J. L. Eur. J. Inorg. Chem. 2006, 3684.
13. Muller, J.; Weyhermuller, T.; Bill, E.; Hildebrandt, P.; Ould-Moussa, L.; Glaser, T.; Wieghardt, K. Angew. Chem, Int. Ed. 1998, 37, 616.
14. 6)(9.1/ν), where ν is the spectrometer frequency (GHz), r is the spin-spin distance (Å), and A ≈ 20 is a numerical constant.
15. Smith, T. D.; Pilbrow, J. R. Coord. Chem. Rev. 1974, 13, 173.
16. Boas, J. F.; Dunhill, R. H.; Pilbrow, J. R.; Srivasta, R. C.; Smith, T. D. J. Chem. Soc. A 1969, 94.
17. Eaton, S. S.; Eaton, G. R.; Chang, C. K. J. Am. Chem. Soc. 1985, 107, 3177.
18. Sokolowski, A.; Leutbecher, H.; Weyhermuller, T.; Schnepf, R.; Both, E.; Bill, E.; Hildebrandt, P.; Wieghardt, K. J. Biol. Inorg. Chem. 1997, 2, 444.
19. Whittaker, M. M.; Whittaker, J. W. J. Biol. Chem. 1988, 263, 6074.
20. After completion of the manuscript, the recently published X-ray structure of SLAC came to our attention ( Skalova, T.; Dohnalek, J.; Ostergaard, L. H.; Ostergaard, P. R.; Kolenko, P.; Duskova, J.; Stepankova, A.; Hasek, J. J. Mol. Biol. 2009, 385, 1165. ). In this structure, the oxygen of Tyr 108 is located at a distance of 4.6 Å from the T2 Cu at the end of a solvent-accessible channel that leads to the TNC. This residue is an obvious candidate as the source of the radical.