Direct electrochemistry of enzymes from the cytochrome P450 2C family |
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| Affiliation: | 1. School of Biomedical Sciences, University of Queensland, Brisbane 4072, Australia;2. Department of Chemistry, University of Queensland, Brisbane 4072, Australia;1. Department of Biological Science, Graduate School of Science, Shizuoka University, Shizuoka 422-8529, Japan;2. Department of Natural Sciences (Biology), School of Medicine, Fukushima Medical University, Fukushima 960-1295, Japan;3. Green Biology Research Division, Research Institute of Green Science and Technology, Shizuoka University, Shizuoka 422-8529, Japan;1. Department of Biological Chemistry, Medical School, National and Kapodistrian University of Athens, 11527 Athens, Greece;2. These authors contributed equally to this work;1. Department of Chemistry, University of Tromsø, The Arctic University of Norway, Postbox 6050 Langnes, N-9037 Tromsø, Norway;2. Arctic Technology Centre, Department of Civil Engineering, Technical University of Denmark, Building 118, 2800 Lyngby, Denmark |
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| Abstract: | The human cytochromes P450 are responsible for the clearance of ∼90% of xenobiotics yet comparatively little is known about their electrochemistry. Here we report the first direct electrochemistry of P450s from the 2C subfamily; one of the major groups of enzymes from this family. Specifically, the proteins that we have examined are recombinant human P450s 2C9, 2C18 and 2C19 and reversible FeIII/II couples are seen in the absence of dioxygen. Even in the presence of trace amounts of dioxygen, a pronounced cathodic response is seen which is assigned to catalytic reduction of the bound dioxygen ligand by the ferrous P450. |
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