Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 9, Issue 2, Pages 152-163Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2005.02.012
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Funding
- NIDDK NIH HHS [DK-31450] Funding Source: Medline
- NIGMS NIH HHS [GM-40392] Funding Source: Medline
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Enzymes containing heme, non-heme iron and copper active sites play important roles in the activation of dioxygen for substrate oxidation. One key reaction step is C-H bond cleavage through H-atom abstraction. On the basis of the ligand environment and the redox properties of the metal, these enzymes employ different methods of dioxygen activation. Heme enzymes are able to stabilize the very reactive iron(IV)-oxo porphyrin-radical intermediate. This is generally not accessible for non-heme iron systems, which can instead use low-spin ferric-hydroperoxo and iron(IV)-oxo species as reactive oxidants. Copper enzymes employ still a different strategy and achieve H-atom abstraction potentially through a superoxo intermediate. This review compares and contrasts the electronic structures and reactivities of these various oxygen intermediates.
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