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BIOCHEMISTRY: An Ancient and Intimate Partnership

Access to the article is free, however registration and sign-in are required. Nonheme iron enzymes can catalyze a wide variety of chemical reactions. Two studies show how this versatility is achieved. Two reports in this issue highlight the biological intimacy of the relation between Fe(II) and dioxygen. On page 453, Kovaleva and Lipscomb (1) show how an enzyme fine-tunes the properties of Fe(II) to activate O2, thereby enabling the oxidation of aromatic diols in a four-electron metabolic process. However, the by-products of molecular oxygen reduction can be highly toxic and need to be removed rapidly. On page 449, Katona et al. (2) reveal details of how one enzyme helps to remove the most toxic by-product, superoxide, by reducing it to the less toxic hydrogen peroxide.

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Classifications


Resource Type: Journal, Review, Diagram
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16

Author and Copyright


Authors and Editors: Carrie M. Wilmot of Department of Biochemistry, University of Minnesota
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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