Making and Breaking the Dioxygen 0-0 Bond: New Insights from Studies of Synthetic Copper Complexes

Accounts of Chemical Research

Volumn 30, Issue 6, 1997, Pages 227-237

  Tolman, William B ^{a,b,c,d,e,f,g}  

^a University of Minnesota   (United States)

^b Wesleyan University ^*  (United States)

^c WESLEYAN UNIVERSITY   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^f UNIVERSITY OF MINNESOTA   (United States)

^g Alfred P Sloan Camille Henry D   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001744285     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar960052m     Document Type: Article

References (88)

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7. Lead references for selected examples of metallooxygenases. Cytochrome P450 (heme-Fe): (a) Cytochrome P-450: Structure, Mechanism, and Biochemistry, 2nd ed.; Ortiz de Montellano, P. R., Ed.; Plenum Press: New York, 1995. (b) Sono, M.; Roach, M. P.; Coulter, E. D.; Dawson, J. H. Chem. Rev. 1996, 96, 2841-2887. Methane monooxygenase and ribonucleotide reductase (nonheme Fe): (c) Lipscomb, J. D. Annu. Rev. Microbiol. 1994, 48, 371-399. (d) Stubbe, J. Adv. Enzymol. 1990, 63, 349-419. (e) Fontecave, M.; Nordlund, P.; Eklund, H.; Reichard, P. Adv. Enzymol. 1992, 65, 147-183. Dopamine β-monooxygenase and peptidylglycine α-amidating monooxygenase (Cu): (f) Klinman, J. P. Chem. Rev. 1996, 96, 2541-2561. Tyrosinase (Cu): (g) Sánchez-Ferrer, A.; Rodríguez-López, J. N.; García-Cánovas, F.; García-Carmona, F. Biochim. Biophys. Acta 1995, 1247, 1-11. (h) Solomon, E. I.; Sundaram, U. M.; Machonkin, T. E. Chem. Rev. 1996, 96, 2563-2605. See also ref 2b.
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