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How to break the rules of dioxygen activation
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Bugg, Tim (2014) How to break the rules of dioxygen activation. Chemistry & Biology, Volume 21 (Number 2). pp. 168-169. doi:10.1016/j.chembiol.2014.01.007 ISSN 1074-5521.
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Official URL: http://dx.doi.org/10.1016/j.chembiol.2014.01.007
Abstract
The activation of dioxygen by oxygenase enzymes is one of the more remarkable reactions in biology, because it has very little chemical precedent; the ability to activate a specific C-H bond by a cytochrome P450 enzyme or break an aromatic ring by a catechol dioxygenase are reactions that are almost impossible in the chemistry laboratory (Bugg, 2003). These enzymes are able to harness the powerful oxidizing capability of dioxygen, the strongest oxidant available in biology, but, in order to do that, they have to activate dioxygen. Because the ground state of gaseous dioxygen is a triplet diradical that is spin forbidden to react via common two-electron reaction mechanisms, it is a relatively inert substance and requires special mechanisms for its activation. Hence, oxygenases usually contain a redox-active metal ion that can transfer a single electron to dioxygen, such as iron (II) or copper (I). Even then, dioxygen activation is not straightforward, because the redox potential for reduction of dioxygen to superoxide is unfavorable, so these enzymes must somehow stabilize the resulting substrate complex. Other oxygenases use an organic cofactor that is able to carry out a 1-electron transfer to dioxygen; thus, the flavin-dependent mono-oxygenases use a reduced flavin cofactor to react with dioxygen, accessing a stable flavin semiquinone intermediate (Bugg, 2003).
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
| Journal or Publication Title: | Chemistry & Biology | ||||
| Publisher: | Cell Press | ||||
| ISSN: | 1074-5521 | ||||
| Official Date: | 20 February 2014 | ||||
| Dates: |
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| Volume: | Volume 21 | ||||
| Number: | Number 2 | ||||
| Page Range: | pp. 168-169 | ||||
| DOI: | 10.1016/j.chembiol.2014.01.007 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Description: | Refers To |
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