Thermodynamics of carbon monoxide photodissociation from the fully reduced cytochrome aa3 oxidase from Rb. sphaeroides

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1757, Issue 3, 2006, Pages 182-188

  Miksovska, Jaroslava ^a   Gennis, Robert B ^b   Larsen, Randy W ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

CO photolysis; Cytochrome c oxidase; Photoacoustic calorimetry; Respiratory protein

Indexed keywords

CARBON MONOXIDE; CYTOCHROME C OXIDASE; HEME DERIVATIVE;

ARTICLE; CALORIMETRY; DISSOCIATION; ENERGY TRANSFER; LIGAND BINDING; NONHUMAN; OBSERVATION; PHOTOACOUSTIC SPECTROSCOPY; PRIORITY JOURNAL; RHODOBACTER SPHAEROIDES; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

ANIMALS; CARBON MONOXIDE; CATTLE; ELECTRON TRANSPORT COMPLEX IV; ESCHERICHIA COLI; HEME; MOLECULAR CONFORMATION; MYOCARDIUM; OXIDATION-REDUCTION; PHOTOBIOLOGY; PHOTOLYSIS; RHODOBACTER SPHAEROIDES; TEMPERATURE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); BOVINAE; RHODOBACTER SPHAEROIDES;

EID: 33646109553     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.01.008     Document Type: Article

References (32)

1. Gennis R.B. Coupled proton and electron transfer reactions in cytochrome oxidase. Front. Biosci. 9 (2004) 581-591
2. Brzezinski P. Redox-driven membrane-bound proton pumps. Trends Biochem Sci. 29 (2004) 380-387
3. Brunori M., Giuffre A., and Sarti P. Cytochrome c oxidase, ligands and electrons. J. Inorg. Biochem. 99 (2005) 324-336
4. Wikstrom M., and Babcock G.T. Catalytic intermediates. Nature 348 (1990) 16-17
5. Larsen R.W., Li W., Copeland R.A., Witt S.N., Lou B.S., Chan S.I., and Ondrias M.R. Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance raman spectroscopy. Biochemistry 29 (1990) 10135-10140
6. Blair D.F., Witt S.N., and Chan S.I. Mechanism of cytochrome c oxidase-catalyzed dioxygen reduction at low-temperatures. Evidence for two intermediates at the three-electron level and entropic promotion of the bond breaking step. J. Am. Chem. Soc. 107 (1985) 7389-7399
7. Hoganson C.W., Pressler M.A., Proshlyakov D.A., and Babcock G.T. From water to oxygen and back again: mechanistic similarities in the enzymatic redox conversions between water and dioxygen. Biochim. Biophys. Acta 1365 (1998) 170-174
8. 2. Biochemistry 36 (1997) 2439-2449
9. Sucheta A., Georgiadis K.E., and Einarsdottir O. Mechanism of cytochrome c oxidase-catalyzed reduction of dioxygen to water: evidence for peroxy and ferryl intermediates at room temperature. J. Biol. Chem. 267 (1997) 10266-10273
10. Fabian M., Wong W.W., Gennis R.B., and Palmer G. Mass spectrometric determination of dioxygen bond splitting in the "Peroxy" intermediate of cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13114-13117
11. Wikstrom M. Energy-dependent reversal of the cytochrome oxidase reaction. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 4051-4054
12. 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
13. Einarsdottir O., Dyer B.R., Lemon D.D., Killough P.M., Hubig S.M., Atherton S.J., Lopez-Garriga J.J., Palmer G., and Woodruff W.H. Photodissociation and recombination of carbonmonoxy cytochrome oxidase: dynamics from picoseconds to kiloseconds. Biochemistry 32 (1993) 12013-12024
14. B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation. Biophys. J. 82 (2002) 1-10
15. Bailey J.A., Tomson F.L., Mecklenburg S.L., MacDonald G.M., Katsonouri A., Puustinen A., Gennis R.B., Woodruff W.H., and Dyer R.B. Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli. Biochemistry 41 (2002) 2675-2683
16. Gennis R.B. Some recent contributions of FTIR difference spectroscopy to the study of cytochrome c oxidase. FEBS Lett. 555 (2003) 2-7
17. Pinakoulaki E., Soulimane T., and Varotsis C. Fourier Transform Infrared (FTIR) and step-scan time resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 Oxidase from Thermus thermophylus. J. Biol. Chem. 277 (2002) 32867-32874
18. Mitchell D.M., Muller J.D., Gennis R.B., and Nienhaus G.U. FTIR study of conformational substrates in the CO adduct of cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 35 (1996) 16782-16788
19. 3 -CO at ambient temperature: evidence from time-resolved Fourier transform infrared spectroscopy. J. Am. Chem. Soc. 124 (2002) 3814-3815
20. B center of bovine heart cytochrome c oxidase. J. Am. Chem. Soc. 125 (2003) 7209-7218
21. 3 from Escherichia coli. J. Am. Chem. Soc. 120 (1998) 8887-8888
22. 3. J. Am. Chem. Soc. 121 (1999) 4495-4499
23. 3. FEBS Lett. 579 (2005) 3014-3018
24. Mitchell D.M., and Gennis R.B. Rapid purification of wild type and mutant cytochrome c oxidase from Rhodobacter sphaeroides by Ni(2+)-NTA affinity chromatography. FEBS Lett. 368 (1995) 148-150
25. Braslavsky S.E., and Heibel G.E. Time-resolved photothermal and photoacoustic methods applied to photoinduced processes in solution. Chem. Rev. 92 (1992) 1381-1410
26. Barker B.D., and Larsen R.W. Photothermal methods applied to energy transducing membrane proteins: a review. J. Biochem. Mol. Biol. Biophys. 5 (2001) 407-434
27. Miksovska J., and Larsen R.W. Structure-function relationships in metalloproteins. In: Marriott G., and Parker I. (Eds). Methods in Enzymology: Biophotonics vol. 360 (2003) 302-329 (part A)
28. Peters K.S., Watson T., and Mar K. Time-resolved photoacoustic calorimetry: a study of myoglobin and rhodopsin. Annu. Rev. Biophys. Chem. 20 (1991) 343-362
29. Miksovska J., Norstrom J., and Larsen R.W. Thermodynamic profiles for CO photodissociation from heme model compounds: effects of proximal ligands. J. Inorg. Chem. 44 (2005) 1006-1014
30. +. Models for the reversible binding of CO to Cu(I) complexes. Inorg. Chem. 20 (1981) 2602-2607
31. 3 heme pocket relaxation subsequent to ligand photolysis from cytochrome c oxidase. J. Am. Chem. Soc. 109 (1987) 5367-5372
32. 3 from Escherichia coli. Is chloride ion a cofactor?. Biochemistry 38 (1999) 7185-7194