The pH-dependent changes of intramolecular electron transfer on copper-containing nitrite reductase

Journal of Biochemistry

Volumn 126, Issue 2, 1999, Pages 408-412

  Kobayashi, Kazuo ^a   Tagawa, Seiichi ^a   Deligeer, ^a   Suzuki, Shinnichiro ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

Intramolecular electron transfer; Nitrite reductase; Pulse radiolysis; Type 1 copper; Type 2 copper

Indexed keywords

BACTERIAL ENZYME; COPPER; NITRITE; NITRITE REDUCTASE; PROTON;

ACHROMOBACTER; ALCALIGENES; ARTICLE; CONTROLLED STUDY; DISSOCIATION CONSTANT; ELECTRON TRANSPORT; ENZYME ACTIVITY; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION STATE; PH; PULSE RADIOLYSIS;

ACHROMOBACTER ALCALIGENES; ACHROMOBACTER CYCLOCLASTES; ACHROMOBACTER XYLOSOXIDANS; ALCALIGENES; ALCALIGENES XYLOSOXIDANS; BACTERIA (MICROORGANISMS);

EID: 0032839514     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022465     Document Type: Article

References (30)

1. Zumft, W.G. (1992) The Denitrifying Prokaryotes in The Prokaryotes, 1 (Balows, A., Truper, H.G., Dworkin, M., and Schleifer, K.-H.) pp. 554-582, Springer-Verlag, Heidelberg
2. Zumft, W.G. and Korner, H. (1997) Enzyme diversity and mosaic gene organization in denitrification. Antonie Van Leeuwenhoek 71, 33-41
3. Godden, J.W., Turley, S., Teller, C., Adman, E.T., Liu, M.Y., Payne, W.J., and LeGall, P.J. (1991) The 2.3 angstrom X-ray structure of nitrite reductaae from Achromobacter cycloclastes. Science 253, 438-442
4. - bound and with Type II copper depleted. J. Biol. Chem. 270, 27458-27454
5. Kukimoto, M., Nishiyama, M., Murphy, M.E., Turley, S., Adman, E.T., Horiuchi, S., and Beppu, T. (1994) X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reductase. Biochemistry 33, 5246-5252
6. Murphy, M.E.P., Turley, S., and Adman, E.T. (1997) Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. J. Biol. Chem. 272, 28455-28460
7. Inoue, T., Gotowda, M., Deligeer, Kataoka, M., Yamaguchi, K., Suzuki, S., Watanabe, H., Gohow, M., and Kai, Y. (1998) Type I Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: Comparison of blue and green nitrite reductase. J. Biochem. 124, 876-879
8. Dodd, F.E., Van Beeumen, J., Eady, R.R., and Hasnain, S.S. (1998) X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partners. J. Mol. Biol. 282, 369-382
9. 1. Cell 81, 369-377
10. Williams, P.A., Fülöp, V., Garman, E.F., Saunders, N.F.W., Ferguson, S.J., and Hajdu, J. (1997) Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature 389, 406-412
11. Nurizzo, D., Sivestrini, M.-C., Mathieu, M., Cutruzzolá, D., Bourgeois, Fülöp, V., Hajdu, J., Brunori, M., Tegnoni, M., and Cambillau, C. (1997) N-terminal arm exchange is observed in the 2.15 Å crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa. Structure 5, 1157-1171
12. Suzuki, S., Kozuma, T., Deligeer, Yamaguchi, K., Nakamura, N., Shidara, S., Kobayashi, K., andTagawa, S. (1994) Pulse radiolysis studies on nitrite reductase from Achromobacter cycloclastes IAM 1013: Evidence for intramolecular electron transfer from type 1 Cu to type 2 Cu. J. Am. Chem. Soc. 116, 11145-11146
13. Suzuki, S., Deligeer, Yamaguchi, K., Kataoka, K., Kobayashi, K., Tagawa, S., Kohzuma,T., Shidara, S., and Iwasaki, H. (1997) Spectroscopic characterization and intramolecular electron transfer process of native and type 2 Cu-depleted nitrite reductase. J. Inorg. Biol. Chem. 2, 265-274
14. Farver, O., Eady, R.R., Abraham, Z.H.L., and Pecht, I. (1998) The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase. FEBS Lett. 436, 239-242
15. Kyritsis, P., Messerschmidt, A., Huber, R., Salmon, A., and Sykes, A.G. (1993) Pulse-radiolysis studies on the oxidised form of the multicopper enzyme ascorbate oxidase: Evidence for two intramolecular electron transfer steps. J. Chem. Soc. Dalton Trans. 731-735
16. Kobayashi, K., Une, H., and Hayashi, K. (1989) Electron transfer process in cytochrome oxidase after pulse radiolysis. J. Biol. Chem. 264, 7976-7980
17. Kobayashi, K., Miki, M., Okamoto, K., and Nishino, T. (1993) Electron transfer process in milk xanthine dehydrogenase as studied by pulse radiolysis. J. Biol. Chem. 268, 24642-24646
18. 1-heme. Biochemistry 36, 13611-13616
19. Kobayashi, K., Tagawa, S., and Mogi, T. (1999) Electron transfer process in cytochrome bd-type ubiquinol oxidase from Escherichia coli revealed by pulse radiolysis. Biochemistry 37, 5913-5917
20. Farver, O. and Pecht, I. (1992) Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase. Proc. Natl. Acad. Sci. USA 89, 8283-8287
21. Farver, O., Wherland, S., and Pecht, I. (1994) Intramolecular electron transfer in ascorbate oxidase is enhanced in the presence of oxygen. J. Biol. Chem. 269, 22933-22936
22. Hille, R. and Anderson, R.F. (1991) Electron transfer in milk xanthine oxidase as studied by pulse radiolysis. J. Biol. Chem. 266, 5608-5615
23. Suzuki, S., Kataoka, K., Yamaguchi, K., Inoue, T., and Kai, Y. (1999) Structure-function relationships of copper-containing nitrite reductases. Coord. Chem. Rev. in press
24. Abraham, Z.H.L., Smith, B.E., Howes, B.D., Lowe, D.J., and Eady, R.R. (1997) pH-dependence for binding a single nitrite ion to each type-2 copper in the copper-containing nitrite reductase of Alcaligenies xylosoxidans. Biochem. J. 324, 511-516
25. Iwasaki, H. and Matsubara, T. (1972) A nitrite reductase from Achromobacter cycloclastes. J. Biochem. 71, 645-652
26. Olesen, K., Veselov, A., Zhao, Y., Wang, B., Danner, B., Scholes, C.P., and Shapleigh, J.P. (1998) Spectroscopic, kinetic, and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3. Biochemistry 37, 6086-6094
27. Veselov, A., Olesen, K., Sienkiewicz, A., Shapleigh, J.P., and Scholes, C.P. (1998) Electronic structural information from Q.Band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase. Biochemistry 37, 6095-6105
28. 2 and C. J. Biol. Chem. 254, 9101-9106
29. Halfen, J.A. and Tolman, W.B. (1994) Synthetic model of the substrate adduct to the reduced active site of copper nitrite reductase, J. Am. Chem. Soc. 116, 5475-5476
30. Ruggiero, C.E., Carrier, S.M., Antholine, W.E., Whittaker, J.W., Cramer, C.J., and Tolman, W.B. (1993) Synthesis and structural and spectroscopic characterization of mononuclear copper nitrosyl complexes: Models for nitric oxide adducts of copper proteins and copper-exchanged zeolites. J. Am. Chem. Soc. 115, 11285-11298