244
Chapter 18 Transition Metal Complexes with CO, N2, NO and O2 Ligands
participate in resonance with the
2
Co(II)O structure (42), with the latter making
the major contribution to the bonding. Similarly, for oxyhemoglobin
2
(HbO ) , the
2
Fe(III)O
structure (48) will participate in resonance with the
2
Fe(II)O structure
(38), but, because the latter structure has three extra bonding electrons, it should
be more stable than structure (48).
The
1
2
S and S = 0 spin wave-functions for the
2
Co(II)O and
2
Fe(II)O
linkages of “increased-valence” structures (42) and (38), with three and four
singly-occupied orbitals, are described in Section 15-2 and in Refs. 20 and 16.
References
1. E.W. Abel, Quart. Revs., 17, 133 (1963).
2. K. Goswami and M.M. Singh, J. Ind. Chem. Soc., 56, 944 (1979).
3. J.C. Chatt, J.R. Dilworth and R.L. Richards, Chem. Revs., 78, 589 (1978).
4. B.R. Davis, N.C. Payne, and J.A. Ibers, J. Amer. Chem. Soc., 91, 1240 (1969); Inorg.
Chem., 8, 2719 (1969).
5. R.D. Harcourt, J. Mol. Struct., 8, 11 (1971).
6. I.M. Treitel, M.T. Flood, R.E. Marsh and H.B. Gray, J. Amer. Chem. Soc., 91, 6512
(1969).
7. B.R. Davis and J.A. Ibers, Inorg. Chem., 9, 2768 (1970).
8. C.G. Pierpont and R. Eisenberg, Inorg. Chem., 11, 1088 (1972).
9. Refs. 1 and 2a-k of J.H. Enemark and R.D. Feltham, Coord. Chem. Revs., 13, 339
(1974).
10. R.D. Harcourt and J.A. Bowden, J. Inorg. Nucl. Chem., 36, 1115 (1974).
11. M.E. Perutz, Nature, 228, 726 (1970).
12. L. Pauling and C.D. Coryell, Proc. Natl. Acad. Sci. U.S.A., 22, 159 (1936).
13. L. Pauling and C.D. Coryell, Proc. Natl. Acad. Sci. U.S.A., 22, 210 (1936).
14. L. Pauling, Proc. Natl. Acad. Sci. U.S.A., 74, 2612 (1977).
15. M. Cerdonio, A. Congiu-Castellano, F. Mogno, B. Pispisa, G.L. Romani and S. Vitale,
Proc. Natl. Acad. Sci. U.S.A., 74, 398 (1977).
16. R.D. Harcourt, Int. J. Quantum Chem., 5, 479 (1971).
17. R.D. Harcourt, Biopolymers, 11, 1551 (1972).
18. R.D. Harcourt, Inor. Nucl. Chem. Letts., 9, 475 (1973).
19. R.D. Harcourt, J. Inorg. Nucl. Chem., 39, 243 (1977).
20. R.D. Harcourt, Int. J. Quantum Chem., Quantum Biol. Symp., 4, 143 (1977).
21. D.S. McClure, Rad. Res. Suppl., 2, 218 (1960).
22. A. Trautwein, H. Eicher, A. Mayer, A. Alfsen, M. Waks, J. Rosa and Y. Beuzard, J.
Chem. Phys., 53, 963 (1970).
23. H. Eicher and A. Trautwein, J. Chem. Phys., 50, 2540 (1969).
24. C.K. Chang and D. Dolphin, Bioorganic Chem. (ed., E.E. Tamelen) Academic Press, 4,
1 (1978).
Chapter 18 Transition Metal Complexes with CO, N2, NO and O2 Ligands
participate in resonance with the
2
Co(II)O structure (42), with the latter making
the major contribution to the bonding. Similarly, for oxyhemoglobin
2
(HbO ) , the
2
Fe(III)O
structure (48) will participate in resonance with the
2
Fe(II)O structure
(38), but, because the latter structure has three extra bonding electrons, it should
be more stable than structure (48).
The
1
2
S and S = 0 spin wave-functions for the
2
Co(II)O and
2
Fe(II)O
linkages of “increased-valence” structures (42) and (38), with three and four
singly-occupied orbitals, are described in Section 15-2 and in Refs. 20 and 16.
References
1. E.W. Abel, Quart. Revs., 17, 133 (1963).
2. K. Goswami and M.M. Singh, J. Ind. Chem. Soc., 56, 944 (1979).
3. J.C. Chatt, J.R. Dilworth and R.L. Richards, Chem. Revs., 78, 589 (1978).
4. B.R. Davis, N.C. Payne, and J.A. Ibers, J. Amer. Chem. Soc., 91, 1240 (1969); Inorg.
Chem., 8, 2719 (1969).
5. R.D. Harcourt, J. Mol. Struct., 8, 11 (1971).
6. I.M. Treitel, M.T. Flood, R.E. Marsh and H.B. Gray, J. Amer. Chem. Soc., 91, 6512
(1969).
7. B.R. Davis and J.A. Ibers, Inorg. Chem., 9, 2768 (1970).
8. C.G. Pierpont and R. Eisenberg, Inorg. Chem., 11, 1088 (1972).
9. Refs. 1 and 2a-k of J.H. Enemark and R.D. Feltham, Coord. Chem. Revs., 13, 339
(1974).
10. R.D. Harcourt and J.A. Bowden, J. Inorg. Nucl. Chem., 36, 1115 (1974).
11. M.E. Perutz, Nature, 228, 726 (1970).
12. L. Pauling and C.D. Coryell, Proc. Natl. Acad. Sci. U.S.A., 22, 159 (1936).
13. L. Pauling and C.D. Coryell, Proc. Natl. Acad. Sci. U.S.A., 22, 210 (1936).
14. L. Pauling, Proc. Natl. Acad. Sci. U.S.A., 74, 2612 (1977).
15. M. Cerdonio, A. Congiu-Castellano, F. Mogno, B. Pispisa, G.L. Romani and S. Vitale,
Proc. Natl. Acad. Sci. U.S.A., 74, 398 (1977).
16. R.D. Harcourt, Int. J. Quantum Chem., 5, 479 (1971).
17. R.D. Harcourt, Biopolymers, 11, 1551 (1972).
18. R.D. Harcourt, Inor. Nucl. Chem. Letts., 9, 475 (1973).
19. R.D. Harcourt, J. Inorg. Nucl. Chem., 39, 243 (1977).
20. R.D. Harcourt, Int. J. Quantum Chem., Quantum Biol. Symp., 4, 143 (1977).
21. D.S. McClure, Rad. Res. Suppl., 2, 218 (1960).
22. A. Trautwein, H. Eicher, A. Mayer, A. Alfsen, M. Waks, J. Rosa and Y. Beuzard, J.
Chem. Phys., 53, 963 (1970).
23. H. Eicher and A. Trautwein, J. Chem. Phys., 50, 2540 (1969).
24. C.K. Chang and D. Dolphin, Bioorganic Chem. (ed., E.E. Tamelen) Academic Press, 4,
1 (1978).