1887

Abstract

Optical changes in - and -type cytochromes, following initiation of the reaction of cytochrome oxidase with O, have been studied in cells and derived membrane particles from oxygen-limited cultures of K12. At successively higher temperatures between − 132 and − 88 °C, the first scan after photolysis of the CO-liganded, reduced oxidase in the presence of O shows a diminution of cytochrome (believed to be an early intermediate in the O reaction) and a slow increase in absorbance at 675 to 680 nm due to an unidentified chromophore. A similar sequence occurs when a single sample is scanned repetitively at − 91 °C. At higher temperatures, oxidation of at least two spectrally distinct cytochromes occurs. Selective photolysis of the cytochrome -CO complex with a He-Ne laser shows that neither of these cytochromes is the CO-binding cytochrome . In all oxidation states examined, no absorbance in the 720 to 860 nm region was observed; it is concluded that both cytochromes and lack redox-active copper that has an environment similar to the copper(s) in mitochondrial cytochrome oxidase.

The amount of cytochrome (but not the amount of reduced cytochrome ) formed after photolysis is directly proportional to the oxygen concentration in the sample at the time of freeze trapping. The results are discussed in relation to the composition and mechanism of action of cytochrome

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1983-05-01
2024-03-28
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References

  1. Aminuddin M., Nicholas D. J. D. 1974; Electron transfer during sulphide and sulphite oxidation in Thiobacillus denitrificans. Journal of General Microbiology 82:115–123
    [Google Scholar]
  2. Austin R. H., Beeson K. W., Eisenstein L., Frauenfelder H., Gunsalus I. C. 1975; Dynamics of ligand binding to myoglobin. Biochemistry 14:5355–5373
    [Google Scholar]
  3. Barrett J. 1956; The prosthetic group of cytochrome a2. Biochemical Journal 64:626–639
    [Google Scholar]
  4. Beinert H., Shaw R. W., Hansen R. E., Hartzell C. R. 1980; Studies on the origin of the near-infrared (800-900 nm) absorption of cytochrome c oxidase. Biochimica et biophysica acta 591:458–470
    [Google Scholar]
  5. Castor L. N., Chance B. 1959; Photochemical determinations of the oxidases of bacteria. Journal of Biological Chemistry 234:1587–1592
    [Google Scholar]
  6. Chance B. 1953; The carbon monoxide compounds of the cytochrome oxidases. I. Difference spectra. Journal of Biological Chemistry 202:383–396
    [Google Scholar]
  7. Chance B. 1981; The cycling of oxygen through intermediates in the cytochrome oxidase-oxygen reaction. In Current Topics in Cellular Regulation 18 pp. 343–360 Estabrook R. W., Srere P. Edited by New York & London: Academic Press.;
    [Google Scholar]
  8. Chance B., Graham N., Legallais V. 1975a; Low temperature trapping method for cytochrome oxidase oxygen intermediates. Analytical Biochemistry 67:552–579
    [Google Scholar]
  9. Chance B., Saronio C., Leigh J. S. 1975b; Functional intermediates in the reaction of membrane- bound cytochrome oxidase with oxygen. Journal of Biological Chemistry 250:9226–9237
    [Google Scholar]
  10. Denis M., Richaud P. 1982; Dynamics of carbon monoxide recombination to fully reduced cytochrome c oxidase in plant mitochondria after low temperature flash photolysis. Biochemical Journal 206:379–385
    [Google Scholar]
  11. De Fonseka K., Chance B. 1980; Oxygen kinetics of frozen cytochrome oxidase. The capacity of the oxygen pocket. Biochemical Journal 185:527–530
    [Google Scholar]
  12. Greenwood C., Barber D., Parr S, Antonim E., Brunori M., Colosimo A. 1978; The reaction of Pseudomonas aeruginosa cytochrome c-551 oxidase with oxygen. Biochemical Journal 173:11–17
    [Google Scholar]
  13. Haddock B. A., Jones C. W. 1977; Bacterial respiration. Bacteriological Reviews 41:47–99
    [Google Scholar]
  14. Hendler R. W., Shrager R. I. 1979; Potentiome- tric analysis of Escherichia coli cytochromes in the optical absorbance range of 500 nm to 700 nm. Journal of Biological Chemistry 254: 11288–11299
    [Google Scholar]
  15. Hoffman P. S., Irwin R. M., Carreira L. A., Morgan T. V., Ensley B. D., Dervartanian D. V. 1980; Studies of photochemical action spectra on N’,N’,N’,N’,-tetramethyl-p-phenylenedi- amine-oxidase-negative mutants of Azotobacter vine- landii. European Journal of Biochemistry 105:177–185
    [Google Scholar]
  16. Jones C. W. 1978; Microbial oxidative phosphorylation. Biochemical Society Transactions 6:361–363
    [Google Scholar]
  17. Kauffman H. F., Van Gelder B. F. 1973a; The respiratory chain of Azotobacter vinelandii. I. Spectral properties of cytochrome d. Biochimica et biophysica acta 305:260–267
    [Google Scholar]
  18. Kauffman H. F., Van Gelder B. F. 1973b; The respiratory chain of Azotobacter vinelandii. II. The effect of cyanide on cytochrome d. Biochimica et biophysica acta 314:276–283
    [Google Scholar]
  19. Kauffman H. F., Van Gelder B. F., Dervartanian D. V. 1980; Effect of ligands on cytochrome d from Azotobacter vinelandii. Journal of Bioenergetics and Biomembranes 12:265–276
    [Google Scholar]
  20. Keilin D. 1933; Supposed direct spectroscopic observation of the “oxygen-transporting ferment”. Nature; London: 132783
    [Google Scholar]
  21. Kuronen T., Ellfolk N. 1972; A new purification procedure and molecular properties of Pseudomonas cytochrome oxidase. Biochimica et biophysica acta 275:308–318
    [Google Scholar]
  22. Lemberg R., Barrett J. 1973; Bacterial cytochromes and cytochrome oxidases. In Cytochromes pp. 217–236 London & New York: Academic Press.;
    [Google Scholar]
  23. Ludwig B. 1980; Heme aa3-type cytochrome coxidases from bacteria. Biochimica et biophysica acta 594:177–189
    [Google Scholar]
  24. Lund T., Raynor J. B. 1975; Electron spin resonance of some bacterial respiratory membranes. Bioenergetics 7:161–166
    [Google Scholar]
  25. Parr S. R., Wilson M. T., Greenwood C. 1975; The reaction of Pseudomonas aeruginosa cytochrome c oxidase with carbon monoxide. Biochemical Journal 151:51–59
    [Google Scholar]
  26. Poole R. K. 1982a; The oxygen reactions of bacterial cytochrome oxidases. Trends in Biochemical Sciences 7:32–34
    [Google Scholar]
  27. Poole R. K. 1982b; The reactions of terminal oxidases in Escherichia coli K12 with oxygen and carbon monoxide at sub-zero temperatures. Biochemical Society Transactions 10:485–488
    [Google Scholar]
  28. Poole R. K., Chance B. 1980; Intermediates in the reaction with oxygen of cytochrome d in oxygen- limited Escherichia coli. First European Bioenergetics Conference Short Reports pp. 107–108 Bologna: Pàtron Editore;
    [Google Scholar]
  29. Poole R. K., Chance B. 1981; The reaction of cytochrome o in Escherichia coli K12 with oxygen. Evidence for a spectrally and kinetically distinct cytochrome o in cells from oxygen-limited cultures. Journal of General Microbiology 126:277–287
    [Google Scholar]
  30. Poole R. K., Lloyd D., Chance B. 1979a; The reaction of cytochrome oxidase with oxygen in the fission yeast Schizosaccharomyces pombe 972h. Biochemical Journal 184:555–563
    [Google Scholar]
  31. Poole R. K., Waring A. J., Chance B. 1979b; Evidence for a functional oxygen-bound intermediate in the reaction of Escherichia coli cytochrome o with oxygen. FEBS Letters 101:56–58
    [Google Scholar]
  32. Poole R. K., Waring A. J., Chance B. 1979c; The reaction of cytochrome o in Escherichia coli with oxygen. Low temperature kinetic and spectral studies. Biochemical Journal 184:379–389
    [Google Scholar]
  33. Poole R. K., Scott R. I., Chance B. 1981; The light-reversible binding of carbon monoxide to cytochrome a, in Escherichia coli K12. Journal of General Microbiology 125:431–438
    [Google Scholar]
  34. Poole R. K., Sivaram A., Salmon I., Chance B. 1982a; Photolysis at very low temperatures of CO- liganded cytochrome oxidase (cytochrome d) in oxygen-limited Escherichia coli. FEBS Letters 141:237–241
    [Google Scholar]
  35. Poole R. K., Salmon I., Sivaram A., Kumar C., Chance B. 1982b; Ligand binding to cytochrome oxidase (cytochrome d) in Escherichia coli: low temperature optical and e.p.r. studies. Second European Bioenergetics Conference Short Reports pp. 145–146 Villeurbanne: L.B.T.M.-C.N.R.S. éditeur;
    [Google Scholar]
  36. Poole R. K., Salmon I., Kumar C., Chance B. 1983; The 650 nm chromophore in Escherichia coli is an ‘oxy-’ or oxygenated compound, not the oxidized form of cytochrome oxidase d: an hypothesis. Journal of General Microbiology 129:1335–1344
    [Google Scholar]
  37. Pudek M. R., Bragg P. D. 1974; Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli. Archives of Biochemistry and Biophysics 164:682–693
    [Google Scholar]
  38. Reid G. A., Ingledew W. J. 1980; The purification of a respiratory oxidase complex from Escherichia coli. FEBS Letters 109:1–4
    [Google Scholar]
  39. Rice C. W., Hempfling W. P. 1978; Oxygen- limited continuous culture and respiratory energy conservation in Escherichia coli. Journal of Bacteriology 134:115–124
    [Google Scholar]
  40. Sivaram A., Chance B., Ching Y. 1982; Low temperature photolysis and recombination kinetics of cytochrome d in Pseudomonas cytochrome oxidase. Federation Proceedings 41:1208
    [Google Scholar]
  41. Wharton D. C., Gibson Q. H. 1976; Cytochrome oxidase from Pseudomonas aeruginosa. IV. Reaction with oxygen and carbon monoxide. Biochimica et biophysica acta 430:445–453
    [Google Scholar]
  42. Wikström M., Krab K., Saraste M. 1981 Cytochrome Oxidase: A Synthesis pp. 117–141 London: Academic Press.;
    [Google Scholar]
  43. Yamanaka T., Okunuki K. 1963; Crystalline Pseudomonas cytochrome oxidase. III. Properties of the prosthetic groups. Biochimica et biophysica acta 67:407–416
    [Google Scholar]
  44. Yaoi H., Tamiya H. 1928; On the respiratory pigment, cytochrome, in bacteria. Proceedings of the Imperial Academy (Japan) 4:436–439
    [Google Scholar]
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