10. ELECTRON TRANSPORT AND OXIDATIVE PHOSPHORYLATION
479
been examined, this transfer is mediated by a respiratory pathway involving cytochromes. Alternate routes for the oxidation of reduced
pyridine nucleotides and flavoproteins exist, but these oxidations do
not support the simultaneous formation of ATP. Similarly, organisms
exist which are devoid of hematin compounds, but oxidative phosphorylation does not appear to be a significant energy-yielding process
in those cells. It seems, therefore, that the oxidative phosphorylation
process associated with the cytochrome respiratory chain may be a
common denominator appearing throughout aerobic organisms. Measurements on the amount of phosphorylation associated with the cyanideinsensitive respiration of certain higher plants are not yet available.
References
1. H. A. Krebs and H. L. Kornberg, Ergeh. Physiol 49, 212-298 (1957).
2. E. Bueding and E. Färber, this volume, Chapter 9.
3. Appearing in another volume in this treatise.
4. C. A. MacMunn, Phil. Trans. Roy. Soc. 177, 267 (1886).
5. D. Keilin, Proc. Roy. Soc. B98, 312-339 (1925).
6. D. Keilin, Ergeh. Enzymforsch.
2, 239-271 (1933).
7. O. Warburg, "Heavy Metals Prosthetic Groups and Enzyme Action" (transl.
A. Lawson). Oxford University Press, London and New York, 1949.
8. O. Warburg and E. Negelein, Biochem. Z. 214, 64-100 (1929).
9. D. Keilin and E. F. Hartree, Proc. Roy. Soc. B125, 171-186 (1938).
10. D. Keilin and E. F. Hartree, Proc. Roy. Soc. B127, 167-191 (1939).
11. A. Fujita and T. Kodama, Biochem. Z. 273, 186-197 (1934).
12. K.-G. Paul, in "The Enzymes" (J. B. Sumner and K. Myrbäck, eds.), Vol.
II, Part 1, pp. 357-396. Academic Press, New York, 1951.
13. B. Chance and G. R. Williams, Advances in Enzymol. 17, 65-134 (1956).
14. W. W. Wainio and S. J. Cooperstein, Advances in Enzymol. 17, 329-392
(1956).
15. E. F. Hartree, Advances in Enzymol. 18, 1-64 (1957).
16. L. Smith, Bacteriol Revs. 18, 106-130 (1954).
17. Appearing in another volume in this treatise.
18. O. Warburg and W. Christian, Biochem. Z. 254, 438-458 (1932); 266, 377411 (1933).
19. O. Warburg and W. Christian, Biochem. Z. 282, 157-205 (1935).
20. H. Theorell, Biochem. Z. 288, 317-337 (1936).
21. E. Haas, B. L. Horecker, and T. R. Hogness, J. Biol. Chem. 136, 747-774
(1940).
22. B. L. Horecker, /. Biol Chem. 183, 593-605 (1950).
23. H. R. Mahler, N. K. Sarkar, L. P. Vernon, and R. A. Alberty, /. Biol. Chem.
199, 585-597 (1952).
24. P. Strittmatter and S. F. Velick, /. Biol. Chem. 228, 785-799 (1957).
25. H. R. Mahler, Advances in Enzymol
17, 233-291 (1956).
26. H. Theorell, in "The Enzymes" (J. B. Sumner and K. Myrbäck, eds.), Vol.
II, Part 1, pp. 335-356. Academic Press, New York, 1951.
27. O. Warburg and W. Christian, Biochem. Z. 242, 206-227 (1931).
28. A. Harden and W. J. Young, Proc. Roy. Soc. B77, 405-420 (1906).
479
been examined, this transfer is mediated by a respiratory pathway involving cytochromes. Alternate routes for the oxidation of reduced
pyridine nucleotides and flavoproteins exist, but these oxidations do
not support the simultaneous formation of ATP. Similarly, organisms
exist which are devoid of hematin compounds, but oxidative phosphorylation does not appear to be a significant energy-yielding process
in those cells. It seems, therefore, that the oxidative phosphorylation
process associated with the cytochrome respiratory chain may be a
common denominator appearing throughout aerobic organisms. Measurements on the amount of phosphorylation associated with the cyanideinsensitive respiration of certain higher plants are not yet available.
References
1. H. A. Krebs and H. L. Kornberg, Ergeh. Physiol 49, 212-298 (1957).
2. E. Bueding and E. Färber, this volume, Chapter 9.
3. Appearing in another volume in this treatise.
4. C. A. MacMunn, Phil. Trans. Roy. Soc. 177, 267 (1886).
5. D. Keilin, Proc. Roy. Soc. B98, 312-339 (1925).
6. D. Keilin, Ergeh. Enzymforsch.
2, 239-271 (1933).
7. O. Warburg, "Heavy Metals Prosthetic Groups and Enzyme Action" (transl.
A. Lawson). Oxford University Press, London and New York, 1949.
8. O. Warburg and E. Negelein, Biochem. Z. 214, 64-100 (1929).
9. D. Keilin and E. F. Hartree, Proc. Roy. Soc. B125, 171-186 (1938).
10. D. Keilin and E. F. Hartree, Proc. Roy. Soc. B127, 167-191 (1939).
11. A. Fujita and T. Kodama, Biochem. Z. 273, 186-197 (1934).
12. K.-G. Paul, in "The Enzymes" (J. B. Sumner and K. Myrbäck, eds.), Vol.
II, Part 1, pp. 357-396. Academic Press, New York, 1951.
13. B. Chance and G. R. Williams, Advances in Enzymol. 17, 65-134 (1956).
14. W. W. Wainio and S. J. Cooperstein, Advances in Enzymol. 17, 329-392
(1956).
15. E. F. Hartree, Advances in Enzymol. 18, 1-64 (1957).
16. L. Smith, Bacteriol Revs. 18, 106-130 (1954).
17. Appearing in another volume in this treatise.
18. O. Warburg and W. Christian, Biochem. Z. 254, 438-458 (1932); 266, 377411 (1933).
19. O. Warburg and W. Christian, Biochem. Z. 282, 157-205 (1935).
20. H. Theorell, Biochem. Z. 288, 317-337 (1936).
21. E. Haas, B. L. Horecker, and T. R. Hogness, J. Biol. Chem. 136, 747-774
(1940).
22. B. L. Horecker, /. Biol Chem. 183, 593-605 (1950).
23. H. R. Mahler, N. K. Sarkar, L. P. Vernon, and R. A. Alberty, /. Biol. Chem.
199, 585-597 (1952).
24. P. Strittmatter and S. F. Velick, /. Biol. Chem. 228, 785-799 (1957).
25. H. R. Mahler, Advances in Enzymol
17, 233-291 (1956).
26. H. Theorell, in "The Enzymes" (J. B. Sumner and K. Myrbäck, eds.), Vol.
II, Part 1, pp. 335-356. Academic Press, New York, 1951.
27. O. Warburg and W. Christian, Biochem. Z. 242, 206-227 (1931).
28. A. Harden and W. J. Young, Proc. Roy. Soc. B77, 405-420 (1906).