Fluoride-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption and EPR spectroscopies

Journal of Biochemistry

Volumn 126, Issue 1, 1999, Pages 98-103

  Tsubaki, Motonari ^a,b   Mogi, Tatsushi ^c   Hori, Hiroshi ^d  

^a UNIVERSITY OF HYOGO   (Japan)

^b INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d OSAKA UNIVERSITY   (Japan)

Author keywords

Cytochrome bd; EPR; Fluoride; Superhyperfine splitting; Ubiquinol oxidase

Indexed keywords

CHLORINE; CYTOCHROME C OXIDASE; FERRIC ION; FLUORIDE; HEME; UBIQUINONE;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING SITE; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; NONHUMAN; OXIDATION REDUCTION REACTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032867283     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022442     Document Type: Article

References (30)

1. Jünemann, S. (1997) Cytochrome bd terminal oxidase. Biochim. Biophys. Acta 1321, 107-127
2. Mogi, T., Tsubaki, M., Hori, H., Miyoshi, H., Nakamura, H., and Anraku, Y. (1998) Two terminal quinol oxidase families in Escherichia coli: Variations on molecular machinery for dioxygen reduction. J. Biochem. Mol. Biol. Biophys. 2, 79-110
3. D'mello, R., Hill, S., and Poole, R.K. (1996) The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: Implications for regulation of activity in vivo by oxygen inhibition. Microbiology 142, 755-763
4. Vavra, M.R., Timkovich, R., Yap, F., and Gennis, R.B. (1986) Spectroscopic studies on heme d in the visible and infrared. Arch. Biochem. Biophys. 250, 461-468
5. Sotiriou, C. and Chang, C.K. (1988) Synthesis of the heme d prosthetic group of bacterial terminal oxidase. J. Am. Chem. Soc. 110, 2264-2270
6. Lorence, R.M. and Gennis, R.B. (1989) Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli. J. Biol. Chem. 264, 7135-7140
7. 2 coordination in a chlorin-containing enzyme by resonance Raman spectroscopy. J. Am. Chem. Soc. 115, 5845-5846
8. Kahlow, M.A., Zuberi, T.M., Gennis, R.B., and Loehr, T.M. (1991) Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy. Biochemistry 30, 11485-11489
9. Hata, A., Kirino, Y., Matsuura, K., Itoh, S., Hiyama, T., Konishi, K., Kita, K., and Anraku, Y. (1985) Assignment of ESR signals of Escherichia coli terminal oxidase complexes. Biochim. Biophys. Acta 810, 62-72
10. Krasnoselskaya, I., Arutjunjan, A.M., Smirnova, I., Gennis, R., and Konstantinov, A.A. (1993) Cyanide-reactive sites in cytochrome bd complex from E. coli. FEBS Lett. 327, 279-283
11. 595 and d in a terminal oxidase of Escherichia coli. Biochim. Biophys. Acta 893, 289-295
12. Hill, J.J., Alben, J.O., and Gennis, R.B. (1993) Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc. Natl. Acad. Sci. USA 90, 5863-5867
13. 595 and d with both carbon monoxide and oxygen. FEMS Microbiol. Lett. 121, 115-120
14. Tsubaki, M., Hori, H., Mogi, T., and Anraku, Y. (1995) Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli. J. Biol. Chem. 270, 28565-28569
15. scc-nitric oxide complexes: Effects of cholesterol and its analogues. Biochemistry 26, 4527-4534
16. Hori, H., Masuya, F., Tsubaki, M., Yoshikawa, S., and Ichikawa, Y. (1992) Electronic and stereochemical characterization of intermediates in the photolysis of ferric cytochrome P450scc nitrosyl complexes. Effects of cholesterol and its analogues on ligand binding structures. J. Biol. Chem. 267, 18377-18381
17. Tsubaki, M., Uno, T., Hori, H., Mogi, T., Nishimura, Y., and Anraku, Y. (1993) Cytochrome d axial ligand of the bd-type terminal quinol oxidase from Escherichia coli. FEBS Lett. 335, 13-17
18. Tsubaki, M., Mogi, T., Anraku, Y., and Hori, H. (1993) Structure of the heme-copper binuclear center of the cytochrome 60 complex of Escherichia coli: EPR and Fourier-transform infrared spectroscopic studies. Biochemistry 32, 6065-6072
19. Hori, H., Tsubaki, M., Mogi, T., and Anraku, Y. (1996) EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli: The proximal axial ligand of heme d is nitrogenous amino acid residue. J. Biol. Chem. 271, 9254-9258
20. Stolzenberg, A.M., Strauss, S.H., and Holm, H.H. (1981) Iron(II, III)-chlorin and -isobacteriochlorin complexes. Models of the heme prosthetic groups in nitrite and sulfite reductases: Means of formation and spectroscopic and redox properties. J. Am. Chem. Soc. 103, 4763-4778
21. Berzofsky, J.A., Peisach, J., and Blumberg, W.E. (1971) Sulf-heme proteins I. Optical and magnetic properties of sulfmyoglobin and its derivatives. J. Biol. Chem. 246, 3367-3377
22. Bracete, A.M., Kadkhodayan, S., Sono, M., Huff, A.M., Zhuang, C., Cooper, D.K., Smith, K.M., Chang, C.K., and Dawson, J.H. (1994) Iron chlorin-reconstituted histidine-ligated heme proteins as models for naturally occurring iron chlorin proteins: Magnetic circular dichroism spectroscopy as a probe of iron chlorin coordination structure. Inorg. Chem. 33, 5042-5049
23. Koland, J.G., Miller, M.J., and Gennis, R.B. (1984) Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli. J. Biol. Chem. 23, 1051-1056
24. Meinhardt, S.W., Gennis, R.B., and Ohnishi, T. (1989) EPR studies of the cytochrome-d complex of Escherichia coli. Biochim. Biophys. Acta 975, 175-184
25. Morimoto, H. and Kotani, M. (1966) Fluorine superhyperfine structure in EPR spectra of the single crystal of the myoglobin fluoride. Biochim. Biophys. Acta 126, 176-178
26. Peisach, J., Blumberg, W.E., Ogawa, S., Rachmilewitz, E.A., and Oltzik, R. (1971) The effects of protein conformation on the heme symmetry in high spin heme proteins as studied by electron paramagnetic resonance. J. Biol. Chem. 246, 3342-3355
27. Rothery, R.A. and Ingledew, W.J. (1989) The cytochromes of anaerobically grown Escherichia coli. An electron-paramagnetic-resonance study of the cytochrome bd complex in situ. Biochem. J. 261, 437-443
28. 558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation. Biochem. J. 308, 641-644
29. Wever, R. and Bakkenist, A.R.J. (1980) The interaction of myeloperoxidase with ligands as studied by EPR. Biochim. Biophys. Acta 612, 178-184
30. 4-containing active center of sulfite reductase in different states of oxidation: Heme activation via reduction-gated exogenous ligand exchange. Biochemistry 36, 12101-12119