Redox control of fast ligand dissociation from Escherichia coli cytochrome bd

Biochemical and Biophysical Research Communications

Volumn 355, Issue 1, 2007, Pages 97-102

  Borisov, Vitaliy B ^a   Forte, Elena ^b   Sarti, Paolo ^b   Brunori, Maurizio ^b   Konstantinov, Alexander A ^a   Giuffrè, Alessandro ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Bacterial respiration; Nitrosative stress; Pathogenicity; Stopped flow spectroscopy

Indexed keywords

BACTERIAL ENZYME; CARBON MONOXIDE; COPPER; CYTOCHROME BD; HEME; LIGAND; NITRIC OXIDE; OXIDOREDUCTASE; OXYGEN; UNCLASSIFIED DRUG;

ANALYTICAL EQUIPMENT; ARTICLE; COMPLEX FORMATION; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; IMMUNE RESPONSE; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; SPECTROSCOPY; STOPPED FLOW SPECTROSCOPY;

CARBON MONOXIDE; CYTOCHROMES; ELECTRON TRANSPORT CHAIN COMPLEX PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEME; KINETICS; LIGANDS; NITRIC OXIDE; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN CONSUMPTION; PROTEIN BINDING; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); ENTEROBACTERIACEAE; ESCHERICHIA COLI;

EID: 33847043904     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.01.118     Document Type: Article

References (30)

1. Anraku Y., and Gennis R.B. The aerobic respiratory chain of Escherichia coli. Trends Biochem. Sci. 12 (1987) 262-266
2. Poole R.K., and Cook G.M. Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation. Adv. Microb. Physiol. 43 (2000) 165-224
3. Baughn A.D., and Malamy M.H. The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen. Nature 427 (2004) 441-444
4. Shi L., Sohaskey C.D., Kana B.D., Dawes S., North R.J., Mizrahi V., and Gennaro M.L. Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration. Proc. Natl. Acad. Sci. USA 102 (2005) 15629-15634
5. Jasaitis A., Borisov V.B., Belevich N.P., Morgan J.E., Konstantinov A.A., and Verkhovsky M.I. Electrogenic reactions of cytochrome bd. Biochemistry 39 (2000) 13800-13809
6. Belevich I., Borisov V.B., Zhang J., Yang K., Konstantinov A.A., Gennis R.B., and Verkhovsky M.I. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proc. Natl. Acad. Sci. USA 102 (2005) 3657-3662
7. Puustinen A., Finel M., Haltia T., Gennis R.B., and Wikstrom M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry 30 (1991) 3936-3942
8. Junemann S. Cytochrome bd terminal oxidase. Biochim. Biophys. Acta 1321 (1997) 107-127
9. Hill J.J., Alben J.O., and Gennis R.B. Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc. Natl. Acad. Sci. USA 90 (1993) 5863-5867
10. Krasnoselskaya I., Arutjunjan A.M., Smirnova I., Gennis R., and Konstantinov A.A. Cyanide-reactive sites in cytochrome bd complex from E. coli. FEBS Lett. 327 (1993) 279-283
11. Borisov V., Arutyunyan A.M., Osborne J.P., Gennis R.B., and Konstantinov A.A. Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands. Biochemistry 38 (1999) 740-750
12. Borisov V.B., Liebl U., Rappaport F., Martin J.-L., Zhang J., Gennis R.B., Konstantinov A.A., and Vos M.H. Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy. Biochemistry 41 (2002) 1654-1662
13. Belevich I., Borisov V.B., Konstantinov A.A., and Verkhovsky M.I. Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability. FEBS Lett. 579 (2005) 4567-4570
14. Hill B.C., Hill J.J., and Gennis R.B. The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli. Biochemistry 33 (1994) 15110-15115
15. Brunori M., Forte E., Arese M., Mastronicola D., Giuffrè A., and Sarti P. Nitric oxide and the respiratory enzyme. Biochim. Biophys. Acta 1757 (2006) 1144-1154
16. MacMicking J., Xie Q.W., and Nathan C. Nitric oxide and macrophage function. Annu. Rev. Immunol. 15 (1997) 323-350
17. Kaysser T.M., Ghaim J.B., Georgiou C., and Gennis R.B. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli. Biochemistry 34 (1995) 13491-13501
18. Miller M.J., and Gennis R.B. Purification and reconstitution of the cytochrome d terminal oxidase complex from Escherichia coli. Methods Enzymol. 126 (1986) 87-94
19. Giuffrè A., Forte E., Brunori M., and Sarti P. Nitric oxide, cytochrome c oxidase and myoglobin: competition and reaction pathways. FEBS Lett. 579 (2005) 2528-2532
20. Eich R.F., Li T., Lemon D.D., Doherty D.H., Curry S.R., Aitken J.F., Mathews A.J., Johnson K.A., Smith R.D., Phillips Jr. G.N., and Olson J.S. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry 35 (1996) 6976-6983
21. Borisov V.B., Forte E., Sarti P., Brunori M., Konstantinov A.A., and Giuffrè A. Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase. FEBS Lett. 580 (2006) 4823-4826
22. Junemann S., Wrigglesworth J.M., and Rich P.R. Effects of decyl-aurachin D and reversed electron transfer in cytochrome bd. Biochemistry 36 (1997) 9323-9331
23. Vos M.H., Borisov V.B., Liebl U., Martin J.-L., and Konstantinov A.A. Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site?. Proc. Natl. Acad. Sci. USA 97 (2000) 1554-1559
24. Sarti P., Giuffrè A., Forte E., Mastronicola D., Barone M.C., and Brunori M. Nitric oxide and cytochrome c oxidase: mechanisms of inhibition and NO degradation. Biochem. Biophys. Res. Commun. 274 (2000) 183-187
25. Gibson Q., and Greenwood C. Reactions of cytochrome oxidase with oxygen and carbon monoxide. Biochem. J. 86 (1963) 541-555
26. Lemon D.D., Calhoun M.W., Gennis R.B., and Woodruff W.H. The gateway to the active site of heme-copper oxidases. Biochemistry 32 (1993) 11953-11956
27. Borisov V.B., Forte E., Konstantinov A.A., Poole R.K., Sarti P., and Giuffrè A. Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide. FEBS Lett. 576 (2004) 201-204
28. Way S.S., Sallustio S., Magliozzo R.S., and Goldberg M.B. Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence. J. Bacteriol. 181 (1999) 1229-1237
29. Endley S., McMurray D., and Ficht T.A. Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection. J. Bacteriol. 183 (2001) 2454-2462
30. Richardson A.R., Dunman P.M., and Fang F.C. The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity. Mol. Microbiol. 61 (2006) 927-939