53 f a cotton and g wilkinson advanced inorganic

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53. F. A. Cotton and G. Wilkinson, Advanced Inorganic Chemistry, Wiley, 5th ed., 1988, pp. 755-775. 54. T. H. Stevens et al., J. Bioi. Chem. 257 (1982), 12106-12113. 55. W. B. Mims et al., J. Bioi. Chem. 255 (1980), 6843-6846. 56. T. H. Stevens et al., Proc. Natl. Acad. Sci USA 76 (1979),3320-3324. 57. T. A. Kent et al., 1. Bioi. Chem. 258 (1983), 8543-8546. 58. J. Cline et al., J. Bioi. Chem. 258 (1983), 5124-5128. 59. T. H. Stevens and S. I. Chan, 1. Bioi. Chem. 256 (1981), 1069-1071. 60. D. H. Chin, G. N. La Mar, and A. Balch, J. Am. Chem. Soc. 102 (1980), 4344-4350. 61. A. L. Balch et al., J. Am. Chem. Soc. 106 (1984),7779-7785. 62. K. D. Karlin and Y. Gultneh, "Binding and Activation of Molecular Oxygen by Copper Complexes" (R), Prog. Inorg. Chem. 35 (1987), 219-327. 63. R. R. Jacobson et al., 1. Am. Chem. Soc. 110 (1988), 3690-3692. 64. N. Kitajima, K. Fujisawa, and Y. Moro-oka, J. Am. Chem. Soc. 111 (1989), 8975-8976. 65. S. Han, Y.-C. Chin, and D. L. Rousseau, Nature 348 (1990), 89-90. 66. L. Que, Jr., "The Catechol Dioxygenases" (R), in Reference 32, pp. 467-524. 67. L. Que, Jr., "Spectroscopic Studies of the Catechol Dioxygenases" (R), 1. Chem. Ed. 62 (1985), 938- 943. 68. J. W. Whittaker et al., 1. Bioi. Chem. 259 (1984), 4466-4475. 69. Y. Tomimatsu, S. Kint, and J. R. Scherer, Biochemistry 15 (1976), 4918-4924. 70. D. H. Ohlendorf, J. D. Lipscomb, and P. C. Weber, Nature 336 (1988), 403-405. 71. D. D. Cox and L. Que, Jr., J. Am. Chem. Soc. 110 (1988),8085-8092. 72. Y. Sawaki and C. S. Foote, 1. Am. Chem. Soc. 105 (1983),5035-5040. 73. P. R. Ortiz de Montellano, ed., Cytochrome P-450: Structure, Mechanism, and Biochemistry (B), Ple- num, 1986. 74. K. Lerch, "Copper Monooxygenases: Tyrosinase and Dopamine j3-Monooxygenase" (R), Metal Ions Bioi. Syst. 13 (1981), 143-186. 75. J. Green and H. Dalton, J. Bioi. Chem. 264 (1989), 17698-17703, and references therein. 76. A. Ericson et al., J. Am. Chem. Soc. 110 (1988),2330-2332. 77. J. E. Colbert, A. G. Katopodis, and S. W. May, J. Am. Chem. Soc. 112 (1990), 3993-3996, and references therein. 78. L. C. Stewart and J. P. Klinman, "Dopamine j3-Hydroxylase of Adrenal Chromaffin Granules: Structure and Function" (R), Annu. Rev. Biochem. 57 (1988),551-592. 79. T. A. Dix and S. J. Benkovic, "Mechanism of Oxygen Activation by Pteridine-Dependent Mono- oxygenases" (R), Ace. Chem. Res. 21 (1988), 101-107. 80. T. L. Poulos, "The Crystal Structure of Cytochrome P-450 cam " (R), in Reference 73, pp. 505-523. 81. T. J. McMurry and J. T. Groves, "Metalloporphyrin Models for Cytochrome PA50" (R), in Reference 73, pp. 1-28. 82. J. T. Groves, T. E. Nemo, and R. S. Myers, J. Am. Chem. Soc. 101 (1979), 1032-1033.
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VIII. REFERENCES 313 83. J. T. Groves, "Key Elements of the Chemistry of Cytochrome P-450: The Oxygen Rebound Mecha- nism" (R), 1. Chem. Ed. 62 (1985), 928-931. 84. D. Dolphin et al., Ann. N.Y. Acad. Sci. 206 (1973),177-200. 85. E. McCandlish et al., 1. Am. Chem. Soc. 102 (1980), 4268-4271. 86. J. N. Burstyn et al., J. Am. Chem. Soc. llO (1988), 1382-1388. 87. J. S. Valentine, J. N. Burstyn, and L. D. Margerum, "Mechanisms of Dioxygen Activation in Metal- Containing Monooxygenases: Enzymes and Model Systems" (R), in Reference 8, pp. 175-187. 88. T. C. Bruice, "Chemical Studies Related to Iron Protoporphyrin-IX Mixed Function Oxidases" (R), in Reference 20, pp. 227-277. 89. T. G. Traylor, W.-P. Fann, and D. Bandyopadhyay, J. Am. Chem. Soc. III (1989), 8009-8010. 90. R. Raag and T. L. Poulos, Biochemistry 28 (1989),7586-7592, and references therein. 91. P. R. Ortiz de Montellano, "Oxygen Activation and Transfer" (R), in Reference 73, pp. 217-271.
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