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Volumn 44, Issue 12, 2005, Pages 1836-1840

A functional model of the cytochrome c oxidase active site: Unique conversion of a heme-μ-peroxo-CuII intermediate into heme-superoxo/CuI

Author keywords

Copper; Heme proteins; Iron; Metalloenzymes; Oxidoreductases

Indexed keywords

COPPER; MATHEMATICAL MODELS; ORGANIC COMPOUNDS; SPECTROSCOPIC ANALYSIS;

EID: 17044434330     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200462582     Document Type: Article
Times cited : (73)

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    • II (-0.61 V versus SCE, DMF) have been reported; TPP = meso-tetraphenylporphinate, TMPA = tris(2-pyridylmethyl)amine; see: a) S. E. Jones, G. S. Srivatsa, D. T. Sawyer, T. G. Traylor, T. C. Mincey, Inorg. Chem. 1983, 22, 3903; b) N. Wei, N. N. Murthy, Q. Chen, J. Zubieta, K. D. Karlin, Inorg. Chem. 1994, 33, 1953.
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    • II (-0.61 V versus SCE, DMF) have been reported; TPP = meso-tetraphenylporphinate, TMPA = tris(2-pyridylmethyl)amine; see: a) S. E. Jones, G. S. Srivatsa, D. T. Sawyer, T. G. Traylor, T. C. Mincey, Inorg. Chem. 1983, 22, 3903; b) N. Wei, N. N. Murthy, Q. Chen, J. Zubieta, K. D. Karlin, Inorg. Chem. 1994, 33, 1953.
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    • note
    • Addition of a trace amount of water to the reaction mixture at low temperature greatly enhances the conversion of the peroxy into the superoxy intermediate.


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