Synthetic models for hemoglobin and myoglobin

Accounts of Chemical Research

Volumn 32, Issue 6, 1999, Pages 455-463

  Collman, James P ^a   Fu, Lei ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; COBALT DERIVATIVE; FERROUS ION; HEME; HEMOGLOBIN; HEMOPROTEIN; IRON OXIDE; MYOGLOBIN; OXYGEN; PORPHYRIN DERIVATIVE;

ARTICLE; CRYSTAL STRUCTURE; ELECTRICITY; HYDROGEN BOND; LIGAND BINDING; OXYGEN AFFINITY; OXYGEN TRANSPORT; OXYGENATION; SYNTHESIS; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 0032837780     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar9603064     Document Type: Article

References (107)

1. Imai, K. Allosteric Effects in Haemoglobin; Cambridge University Press: Cambridge, 1982.
2. Ackers, G. K.; Doyle, M. L.; Myers, D.; Daugherty, M. A. Molecular Code for Cooperativity in hemoglobin. Science 1992, 255, 54-63.
3. Stryer, L. Biochemistry, 4th ed.; W. H. Freeman & Co.: New York, 1995.
4. Wang, J. H.; Nakahara, A.; Fleischer, E. B. Hemoglobin Studies. I. The Combination of Carbon Monoxide with Hemoglobin and Related Model Compounds. J. Am. Chem. Soc. 1958, 80, 1109-1112.
5. Pauling, L. Nature of the Iron-Oxygen Bond in Oxyhaemoglobin. Nature 1964, 203, 182-183.
6. Yonetani, T.; Yamamoto, H.; Itizuka, T. Studies on Cobalt Myoglobins and Hemoglobins. 3. Electron-Paramagnetic Resonance Studies of Reversible Oxygenation of Cobalt Myoglobins and Hemoglobins. J. Biol. Chem. 1974, 249, 2168-2174.
7. Ikeda-Saito, M.; Bruniori, M.; Yonetani, T. Cobalt Myoglobins and Hemoglobins. 7. Oxygenation and EPR Spectral Properties of Aplysia Myoglobins Containing Cobaltous Porphyrins. Biochim. Biophys. Acta 1978, 533, 173-180.
8. Kitagawa, T.; Ohfrias, M. R.; Rousseau, D. L.; Ikeda-Saito, M.; Yonetani, T. Evidence for Hydrogen-Bonding of Bound Dioxygen to the Distal Histidine of Oxycobalt Myoglobin and Hemoglobin. Nature 1982, 290, 869-871.
9. Phillips, S. E. V. Structure and Refinement of Oxymyoglobin At 1.6 Å Resolution. J. Mol. Biol. 1980, 142, 531-554.
10. Phillips, S. E. V.; Schoenborn, B. P. Neutron Diffraction Reveals Oxygen-Histidine Hydrogen Bond in Oxymyoglobin. Nature 1981, 292, 81-82.
11. Wittenberg, J. B.; Appleby, C. A.; Wittenberg, B. A. Kinetics of the Reactions of Leghemoglobin with Oxygen and Carbon Monoxide. J. Biol. Chem. 1972, 247, 527-531.
12. Kloek, A. P.; Yang, J.; Mathews, F. S.; Goldberg, D. E. Expression, Characterization, and Crystallization of Oxygen-Avid Ascaris Hemoglobin Domains. J. Biol. Chem. 1993, 260, 17669-17671.
13. Yang, J.; Kloek, A. P.; Glodberg, D. E.; Mathews, F. S. The Structure of Ascaris Hemoglobin Domain-I at 2.2 Å Resolution: Molecular Features of Oxygen Avidity. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 4224-4228.
14. Huang, S. C.; Huang, J.; Kloek, A. P.; Goldberg, D. E.; Friedman, J. M. Hydrogen-Bonding of Tyrosine B10 to Heme-Bound Oxygen in Ascaris Hemoglobin: Direct Evidence from UV Resonance Raman Spectroscopy. J. Biol. Chem. 1996, 271, 958-962.
15. Stone, J. R.; Sands, R. H.; Dunham, W. R.; Marietta, M. A. Electron Paramagnetic Resonance Spectral Evidence for the Formation of a Pentacoordinate Nitrosyl-heme Complex on Soluble Guanylate Cyclase. Biochem. Biophys. Res. Commun. 1995, 207, 572-577.
16. Decatur, S. M.; Franzen, S.; DePillis, G. D.; Dyer, R. B.; Woodruff, W. H.; Boxer, S. G. Trans Effects in Nitric Oxide Binding to Myoglobin Cavity Mutant H93G. Biochemistry 1996, 35, 4939-4944.
17. Hirota, S.; Ogura, T.; Shinzawaitoh, K.; Yoshikawa, S.; Kitagawa, T. Observation of Multiple CN-Isotope-Sensitive Raman Bands for CN-Adducts Of Hemoglobin, Myoglobin, and Cytochrome c Oxidase - Evidence for Vibrational Coupling Between the Fe-C-N Bending and Porphyrin In-Plane Modes. J. Phys. Chem. 1996, 100, 15274-15279.
18. Reddy, K. S.; Yonetani, T.; Tsuneshige, A.; Chance, B.; Kushkuley, B.; Stavrov, S. S.; Vanderkooi, J. M. Infrared Spectroscopy of the Cyanide Complex of Iron(II) Myoglobin and Comparison with Complexes of Microperoxidase and Hemoglobin. Bio-chemistry 1996, 35, 5562-5570.
19. Coburn, R. F. Carbon Monoxide Body Stores. Ann. N. Y. Acad. Sci. 1970, 174, 11-22.
20. Fermi, G.; Perutz, M. F. In Haemoglobin and Myoglobin. Atlas of Biological Structures; Phillips, D. C., Richards, F. M., Eds.; Clarendon: Oxford, 1981.
21. Dickerson, R. E.; Geis, I. Hemoglobin; Benjamin Cummings: Menlo Park, CA, 1983.
22. Perutz, M. F.; Fermi, G.; Luisi, B.; Shaanan, B.; Liddungton, R. C. Stereochemistry of Cooperative Mechanisms in Hemoglobin. Acc. Chem. Res. 1987, 20, 309-321.
23. Lambright, D. G.; Balasubramanian, S.; Boxer, S. G. Protein Relaxation Dynamics in Human Myoglobin. Chem. Phys. 1991, 158, 249-260.
24. Burstyn, J. N.; Yu, A. E.; Dierks, E. A.; Hawkins, B. K; Dawson, J. H. Studies of the Heme Coordination and Ligand Binding Properties of Soluable Guanylyl Cyclase (sGC): Characterization of Fe(II)sGC and Fe(II)sGC(CO) by Electronic Absorption and Magnetic Circular Dichroism Spectroscopies and Failure of CO to Activate the Enzyme. Biochemistry 1995, 34, 5896-5903.
25. 2 and CO Binding to Metalloporphyrins and Heme Proteins. Proc. Natl. Acad. Sci. U.S.A. 1976, 73, 3333-3337.
26. Collman, J. P.; Brauman, J. I.; Doxsee, K. M. Carbon Monoxide Binding to Iron Porphyrins. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 6035-6039.
27. Balasubramanian, S.; Lambright, D. G.; Simmons, J. H.; Gill, S. J.; Boxer, S. G. Determination of the Carbon Monoxide Binding Constants of Myoglobin Mutants: Comparison of Kinetic and Equilibrium Methods. Biochemistry 1994, 33, 8355-8360.
28. Heidner, E. J.; Ledner, R. C.; Perutz, M. F. Structure of Horse Carbon Monoxyhaemoglobin. J. Mol. Biol. 1976, 104, 707-722.
29. Kuriyan, J.; Wilz, S.; Karplus, M.; Petsko, G. A. X-ray Structure and Refinement of Carbon-monoxy Fe-(II)-myoglobin at 1.5 Å Resolution. J. Mol. Biol. 1986, 192, 133-154.
30. Derewenda, Z.; Dodsong, E. P.; Emsley, P.; Harris, D.; Nagai, K.; Perutz, M. F.; Reanud, J. P. Stereo-chemistry of Carbon Monoxide Binding to Normal Human Adult and Cowtown Haemoglobins. J. Mol. Biol. 1990, 211, 515-519.
31. Cheng, K; Schoenborn, B. P. Neutron Diffraction Study of Carbon Monoxymyoglobin. J. Mol. Biol. 1991, 220, 381-399.
32. Quillin, M. L.; Arduini, R. M.; Olson, J. S.; Phillips, G. N. High-Resolution Crystal Structures of Distal Histidine Mutants of Sperm Whale Myoglobin. J. Mol. Biol. 1993, 234, 140-155.
33. Teng, T.-Y.; Srajer, V.; Moffat, K. Photolysis-Induced Structural Changes in Single Crystals of Carbonmonoxy Myoglobin at 40 K. Nat. Struct. Biol. 1994, 1, 701-703.
34. Schlichting, I.; Berendzed, J.; Phillips, J.; Sweet, R. M. Crystal Structure of Photolysed Carbonmonoxymyoglobin. Nature 1994, 371, 808-812.
35. Ivanov, D.; Sage, J. T.; Keim, M.; Powel, J. R.; Asher, S. A.; Chempion, P. M. Determination of CO Orientation in Myoglobin by Single-Crystal Infrared Linear Dichrosim. J. Am. Chem. Soc. 1994, 116, 4139-4140.
36. Lim, M.; Jackson, T. A.; Anfinrud, P. A. Binding of CO to Myoglobin from a Heme Pocket Docking Site to Form Nearly Linear Fe-C-O. Science 1995, 269, 962-966.
37. Lim, M.; Jackson, T. A.; Anfinrud, P. A. Modulating Carbon Monoxide Binding Affinity and Kinetics in Myoglobin: the Roles of the Distal Histidine and Heme Pocket Docking Site. J. Biol. Inorg. Chem. 1997, 2, 531-536.
38. Ghosh, A.; Bocian, D. F. Carbonyl Tilting and Bending Potential Energy Surface of Carbon Monoxyhemes. J. Phys. Chem. 1996, 100, 6363-6367.
39. Vangberg, T.; Bocian, D. F.; Ghosh, A. Deformability of Fe(II)CO and Fe(III)CN Groups in Heme Protein Models: Nonlocal Density Functional Theory Calculations. J. Biol. Inorg. Chem. 1997, 2, 526-530.
40. Spiro, T. G.; Kozlowski, P. M. Will the Real FeCO Please Stand Up? J. Biol. Inorg. Chem. 1997, 2, 516-520.
41. Spiro, T. G.; Kozlowski, P. M. Disordant Results on FeCO Deformability in Heme Proteins Reconciled by Density Functional Theory. J. Am. Chem. Soc. 1998, 120, 4524-4525.
42. Sage, J. T. Myoglobin and CO: Structure, Energetics, and Disorder. J. Biol. Inorg. Chem. 1997, 2, 537-543.
43. Sage, J. T. Infrared Crystallography: Structural Refinement Through Spectroscopy. Appl. Spectrosc. 1997, 51, 568-573.
44. Springer, B. A.; Sligar, S. G.; Olson, J. S.; Phillips, G. N., Jr. Mechanisms of Ligand Recognition in Myoglobin. Chem. Rev. 1994, 94, 699-714.
45. Cameron, A. D.; Smerdon, S. J.; Wilkinson, A. J.; Habash, J.; Helliwell, J. R.; Li, T.; Olson, J. S. Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of a Threonine68-(E11) Mutant Investigated by X-ray Crystallography and Infrared Spectroscopy. Biochemistry 1993, 32, 13061-13070.
46. Hargrove, M. S.; Singleton, E. W.; Quillin, M. L.; Ortiz, L. A.; Phillips, G. N. J.; Olson, J. S. His64(E7) → Tyr Apomyoglobin as a Reagent for Measuring Rates of Hemin Dissociation. J. Biol. Chem. 1994, 269, 4207-4214.
47. Jameson, G. B. In Metal-Containing Polym. Materials; Carraher, C., Zeldin, M., Sheats, J., Culbertson, B., Pittman, C. U., Jr., Eds.; Plenum: New York, 1996; pp 421-468.
48. Momenteau, M.; Reed, C. A. Synthetic Heme Dioxygen Complexes. Chem. Rev. 1994, 94, 659-698.
49. Jameson, G. B.; Ibers, J. A. On Carbon Monoxide and Dioxygen Binding by Iron(II) Porphyrinato Systems. Comments Inorg. Chem. 1983, 2, 97-126.
50. Huang, X.; Boxer, S. G. Discovery of New Ligand Binding Pathways in Myoglobin by Random Mutagenesis. Nat. Struct. Biol. 1994, 1, 226-229.
51. 2 by Myohemerythrin. Evidence for Different Rate-Determining Steps and a Caveat. J. Am. Chem. Soc. 1995, 117, 11993-11994.
52. Collman, J. P.; Reed, C. A. Syntheses of Ferrous Porphyrin Complexes: A Hypothetical Model for Deoxymyoglobin. J. Am. Chem. Soc. 1973, 95, 2048-2049.
53. Collman, J. P. Synthetic Models for the Oxygen-Binding Hemoproteins. Acc. Chem. Res. 1977, 10, 265-272.
54. Collman, J. P.; Brauman, J. I.; Doxsee, K. M.; Halbert, T. R.; Suslick, K. S. Model Compounds for the T State of Hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1978, 75, 564-568.
55. 2 Binding to Iron Porphyrins. Proc. Natl. Acad. Sci. U.S.A. 1978, 75, 1052-1055.
56. Collman, J. P.; Brauman, J. I.; Rose, E.; Suslick, K. S.; Ibers, J. A.; Jameson, G. B.; Molinaro, F. S. Structural Changes Upon Oxygenation of an Iron-(II)(porphyrinato)(imidazole) Complex. J. Am. Chem. Soc. 1978, 100, 6769-6770.
57. Jones, R. D.; Summerville, D. A.; Basolo, F. Synthetic Oxygen Carriers Related to Biological Systems. Chem. Rev. 1979, 79, 139-179.
58. Collman, J. P.; Halbert, T. R.; Suslick, K. S. In Metal Ion Activation of Dioxygen; Spiro, T. G., Ed.; Wiley: New York, 1980; Chapter 1.
59. Traylor, T. G. Synthetic Model Compounds for Hemoproteins. Acc. Chem. Res. 1981, 14, 102-109.
60. Scheldt, W. R.; Reed, C. A. Spin-State/Stereochemical Relationships in Iron Porphyrins: Implications for the Hemoproteins. Chem. Rev. 1981, 81, 543-555.
61. Niederhoffer, E. C.; Timmons, J. H.; Martell, A. E. Thermodynamics of Oxygen Binding in Natural and Synthetic Dioxygen Complexes. Chem. Rev. 1984, 84, 137-203.
62. Baldwin, J. E.; Perlmutter, P. In Topics in Current Chemistry, Boschke, F. L., Ed.; Springer: Berlin, 1984; p 181.
63. 2 Binding Heme Proteins. J. Chem. Educ. 1985, 62, 974-983.
64. Woolery, G. L.; Walters, M. A.; Suslick, K. S.; Powers, L. S.; Spiro, T. G. Alternative Iron-Dioxygen Bond Lengths in Dioxygen Adducts of Iron Porphyrins: Implications for Hemoglobin Cooperativity. J. Am. Chem. Soc. 1985, 707, 2370-2373.
65. 2 Binding to Iron Porphyrins: Polar Pocket Effects. J. Am. Chem. Soc. 1985, 107, 6504-6510.
66. Momenteau, M. Synthesis and Coordination Properties of Superstructured Iron Porphyrins. Pure Appl. Chem. 1986, 58, 1493-1502.
67. Tétreau, C.; Momenteau, M.; Lavalette, D. Influence of Distal Steric Hindrance on Multiple Energy Barriers in Ligand-Binding to Heme Model Compounds. Inorg. Chem. 1990, 29, 1727-1731.
68. 2 and CO to Heme Protein Models. Tetrahedron Lett. 1993, 34, 7267-7270.
69. Collman, J. P.; Zhang, X.; Wong, K.; Brauman, J. I. Dioxygen Binding in Iron and Cobalt Picnic Basket Prophyrins. J. Am. Chem. Soc. 1994, 116, 6245-6251.
70. Tétreau, C.; Lavalette, D.; Momenteau, M.; Fischer, J.; Weiss, R. Structure-Function Relationship in Oxygen and Carbon Monoxide Binding with Heme Models. Biophys. J. 1994, 66, A262-A262.
71. Gerothanassis, I. P.; Barrie, P. J.; Momenteau, M.; Hawkes, G. E. Solid State C-13 NMR Evidence for a Large Deviation from Linearity of the Fe-CO Unit in the CO Complex with Myoglobin. J. Am. Chem. Soc. 1994, 116, 11944-11949.
72. Collman, J. P.; Gagne, R. R.; Halbert, T. R.; Marchon, J. C.; Reed, C. A. Reversible Oxygen Adduct Formation in Ferrous Complexes Derived from a 'Picket Fence' Porphyrin: A Model for Oxymyoglobin. J. Am. Chem. Soc. 1973, 95, 7868-7870.
73. Collman, J. P.; Gagne, R. R.; Reed, C. A.; Halbert, T. R.; Lang, G.; Robinson, W. T. Picket fence Porphyrins - Synthetic Models for Oxygen Binding Hemoproteins. J. Am. Chem. Soc. 1975, 97, 1427-1439.
74. Jameson, G. B.; Rodley, G. A.; Robinson, W. T.; Gagne, R. R.; Reed, C. A.; Collman, J. P. Structure of a Dioxygen Adduct of (1-Methylimidazole)-mesotetrakis(α,α,α,α-o- pivalamidophenyl) porphinato iron(II). Inorg. Chem. 1978, 17, 850-857.
75. Jameson, G. B.; Molinaro, F. S.; Ibers, J. A.; Collman, J. P.; Brauman, J. L; Rose, E.; Suslick, K. S. Models for the Active Site of Oxygen-Binding Hemoproteins: Dioxygen Binding Properties and the Structures of (2-Methylimidazole)(meso)-tetra-(α,α,α,α-o- pivalaminophenyl)porphyrinatoiron(II)-Ethanol and its Dioxygen Adduct. J. Am. Chem. Soc. 1980, 102, 3224-3237.
76. Collman, J. P.; Gagne, R. R.; Reed, C. A.; Robinson, W. R.; Rodley, G. A. Structure of an Iron(II) Dioxygen Complex: A Model for Oxygen Carrying Hemoproteins. Proc. NatL Acad. Sci. U.S.A. 1974, 71, 1326-1329.
77. Collman, J. P.; Gagne, R. R.; Kouba, J.; Ljusberg-Wahren, H. Reversible Oxygen Adduct Formation in Co(II) "Picket Fence" Porphyrins. J. Am. Chem. Soc. 1974, 96, 6800-6802.
78. Collman, J. P.; Brauman, J. I.; Doxsee, K. M.; Halbert, T. R.; Hayes, S. E.; Suslick, K. S. Oxygen Binding to Cobalt Porphyrins. J. Am. Chem. Soc. 1978, 100, 2761-2766.
79. Collman, J. P.; Brauman, J. I.; Doxsee, K. M.; Halbert, T. R.; Bunnenberg, E.; Linder, R. E.; La Mar, G. N.; Del Gaudio, J.; Lang, G.; Spartalian, K. Synthesis and Characterization of "Tailed Picket Fence" Porphyrins. J. Am. Chem. Soc. 1980, 102, 4182-4192.
80. Collman, J. P.; Brauman, J. L; Collins, T. J.; Iverson, B.; Sessler, J. L. The Pocket Porphyrin: A Hemoprotein Model with Lowered CO Affinity. J. Am. Chem. Soc. 1981, 703, 2450-2452.
81. Collman, J. P.; Brauman, J. L; Collins, T. J.; Iverson, B. L.; Lang, G.; Pettman, R. G.; Sessler, J. L; Walters, M. A. Synthesis and Characterization of the 'Pocket' Porphyrins. J. Am. Chem. Soc. 1983, 105, 3038-3052.
82. 2 and CO Binding to Iron(II) Porphyrins: A Comparison of the "Picket Fence" and "Pocket" Porphyrins. J. Am. Chem. Soc. 1983, 105, 3052-3064.
83. Kim, K. F., J.; Sessler, J. L.; Cyr, M.; Hugdahl, J.; Collman, J. P.; Ibers, J. A. Structural Charcterization of a Sterically Encumbered Iron(II) Porphyrin CO Complex. J. Am. Chem. Soc. 1989, 111, 403-405.
84. Tétreau, C.; Lavalette, D.; Momenteau, M.; Fischer, J.; Weiss, R. Structure-Reactivity Relationship in Oxygen and Carbon Monoxide Binding with Some Heme Models. J. Am. Chem. Soc. 1994, 116, 11840-11848.
85. Hashimoto, T.; Dyer, R. T.; Crossley, M. J.; Baldwin, J. E.; Basolo, F. Ligand, Oxygen, and Carbon-Monoxide Affinities of Iron(II) Modified Capped Porphyrins. J. Am. Chem. Soc. 1982, 104, 2101-2109.
86. 2 Binding Properties ospirof Novel 4-Atom-Linked Capped Porphyrins. J. Am. Chem. Soc. 1991, 113, 3998-4000.
87. Johnson, M.; Seok, W. K.; Ma, W.; Slebodnick, C.; Wilcosen, K. M.; Ibers, J. A. Four-Atom-Linked Capped Porphyrins: Synthesis and Characterization. J. Org. Chem. 1996, 61, 3298-3303.
88. 2Im). Inorg. Chem. 1996, 35, 3607-3613.
89. Slebodnick, C.; Fettinger, J. C.; Peterson, H. B.; Ibers, J. A. Structural Characterization of 5 Sterically Protected Porphyrins. J. Am. Chem. Soc. 1996, 118, 3216-3224.
90. 2 and CO. J. Biol. Inorg. Chem. 1997, 2, 521-525.
91. Collman, J. P.; Zhang, X.; Herrman, P. C.; Uffelman, E. S.; Boitrel, B.; Straumanis, A.; Brauman, J. I. Congruent Multiple Michael Addition for the Synthesis of Biomimetic Heme Analogues. J. Am. Chem. Soc. 1994, 116, 2681-2682.
92. Collman, J. P.; Boitrel, B.; Fu, L.; Galanter, J.; Straumanis, A.; Rapta, M. The Chloroacetamido Group as a New Linker for the Synthesis of Hemoprotein Analogues. J. Org. Chem. 1997, 62, 2308-2309.
93. Collman, J. P.; Wang, Z.; Straumanis, A. Isocyanate as a Versatile Synthon for Modular Synthesis of Functionalized Porphyrins. J. Org. Chem. 1998, 63, 2424-2425.
94. Collman, J. P.; Herrmann, P. C.; Fu, L.; Eberspacher, T. A.; Eubanks, M.; Boitrel, B.; Hayoz, P.; Zhang, X.; Brauman, J. I. Aza-crown Capped Porphyrin Models of Myoglobin: Studies of the Steric Interactions of Gas Binding. J. Am. Chem. Soc. 1997, 119, 3481-3489.
95. La Mar, G. N.; Eaton, G. R.; Holm, R. H.; Walker, F. A. Proton Magnetic Resonance Investigation of Antiferromagnetic Oxo-bridged Ferric Dimers and Related High-spin Monomeric Ferric Complexes. J. Am. Chem. Soc. 1973, 95, 63-75.
96. La Mar, G. N.; Walker, F. A. Proton Nuclear Magnetic Resonance and Electron Spin Resonance Investigation of the Electronic Structure and Magnetic Properties of Synthetic Low-spin Ferric Porphyrins. J. Am. Chem. Soc. 1973, 95, 1782-1790.
97. Goff, H.; La Mar, G. N. High-spin Ferrous Porphyrin Complexes as Models for Deoxymyoglobin and -Hemoglobin. A proton Nuclear Magnetic Resonance Study. J. Am. Chem. Soc. 1977, 99, 6599-6606.
98. Goff, H.; La Mar, G. N.; Reed, C. A. Nuclear Magnetic Resonance Investigation of Magnetic and Electronic Properties of "Intermediate Spin" Ferrous Porphyrin Complexes. J. Am. Chem. Soc. 1977, 99, 3641-3646
99. Ray, G. B.; Li, X. Y.; Ibers, J. A.; Sessler, J. L.; Spiro, T. G. How Far Can Proteins Bend the FeCO Unit? Distal Polar and Steric Effects in Heme Proteins and Models. J. Am. Chem. Soc. 1994, 116, 162-176.
100. Spiro, T. G. CO Binding and Bending Energetics Science 1995, 270, 221-221.
101. Jaquinod, L; Prevot, L.; Fisher, J.; Weiss, R. Biphenyl-Strapped Diphenylporphyrins: Synthesis and Spectroscopic Characterization of a Series of Porphyrins with Ether-Linked Straps: Preliminary CO Binding-Properties of Their Iron(II) Derivatives. Inorg. Chem. 1998, 37, 1142-1149.
102. Momenteau, M.; Lavalette, D. Kinetic Evidence for Dioxygen Stabilization in Oxygenated Iron(II)-Porphyrins by Distal Polar Interactions. J. Chem. Soc., Chem. Commun. 1982, 341-343.
103. Mispelter, M.; Momenteau, M.; Lavalette, D.; Lhoste, J.-M. Hydrogen-Bond Stabilization of Oxygen in Hemoprotein Models. J. Am. Chem. Soc. 1983, 705, 5165-5166.
104. Lavalette, D.; Tétreau, C.; Mispelter, M.; Momenteau, M.; Lhoste, J.-M. Linear Free-Energy Relationships in Binding of Oxygen and Carbon-Monoxide with Heme Model Compounds and Heme-Proteins Eur. J. Biochem. 1984, 145, 555-565.
105. Chang, C. K.; Ward, B.; Young, R.; Kondylis, M. P. Fine Tuning Of Heme Reactivity: Hydrogen-Bonding and Dipole Interactions Affecting Ligand-Binding to Hemoproteins. J. Macromol. Sci. Chem 1988, A25, 1307-1326.
106. Wuenschell, G. E.; Tétreau, C.; Lavalette, D.; Reed, C. A. H-Bonded Oxyhemoglobin Models with Substituted Picket-Fence Porphyrins: The Model Compound Equivalent of Site-Directed Mutagenesis. J. Am. Chem. Soc. 1992, 114, 3346-3355.
107. Collman, J. P.; Fu, L.; Zingg, A.; Diederich, F. Dioxygen and Carbon Monoxide Binding in Dendritic Iron(II) Porphyrins. Chem. Commun. 1997, 193-194.