Abstract

We studied the selectivity of a functional model of cytochrome c oxidase's active site that mimics the coordination environment and relative locations of Fe a3 , Cu B , and Tyr 244 . To control electron flux, we covalently attached this model and analogs lacking copper and phenol onto self-assembled monolayer–coated gold electrodes. When the electron transfer rate was made rate limiting, both copper and phenol were required to enhance selective reduction of oxygen to water. This finding supports the hypothesis that, during steady-state turnover, the primary role of these redox centers is to rapidly provide all the electrons needed to reduce oxygen by four electrons, thus preventing the release of toxic partially reduced oxygen species.

Keywords

ChemistryRedoxElectron transferOxygenCytochrome c oxidaseElectron transport chainPhotochemistryCopperOxidase testCytochrome cInorganic chemistryMitochondrionOrganic chemistryBiochemistryEnzyme

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Publication Info

Year
2007
Type
article
Volume
315
Issue
5818
Pages
1565-1568
Citations
546
Access
Closed

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James P. Collman, Neal K. Devaraj, Richard A. Decréau et al. (2007). A Cytochrome c Oxidase Model Catalyzes Oxygen to Water Reduction Under Rate-Limiting Electron Flux. Science , 315 (5818) , 1565-1568. https://doi.org/10.1126/science.1135844

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DOI
10.1126/science.1135844