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Frontiers beyond the hydroxylation paradigm in the diverse chemistry of non‐heme Fe(IV)‐oxo (ferryl) enzyme intermediates (110.2)
Author(s) -
Bollinger J.
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.110.2
Subject(s) - chemistry , hydroxylation , enzyme , bond cleavage , radical , heme , epoxide , stereochemistry , combinatorial chemistry , photochemistry , catalysis , organic chemistry
Non‐heme‐iron (NH‐Fe) enzymes activate O 2 for an impressive array of biomedically, agriculturally, and environmentally important oxidation reactions. Our past decade's work has characterized iron(IV)‐oxo (Fe IV =O or ferryl) complexes in the reactions of several such NH‐Fe enzymes. 1 In five of these enzymes, the ferryl complexes generate substrate radicals by abstracting hydrogen (H•) from aliphatic carbons, 2‐6 leading to formation of new C‐O, 2‐4 C‐Cl/Br, 5,6 and C‐S bonds. 1 Motivated by our success in rationalizing the divergent outcomes of the NH‐Fe α‐ketoglutarate‐dependent aliphatic hydroxylases and halogenases, 7 we now seek both to exploit the ferryl manifold for novel, unnatural carbon‐functionalization reactions and to explain the structural and mechanistic bases for several other natural reaction types, including 1,3‐dehydrogenation of an alcohol to epoxide, 8 stereo‐inversion of a chiral carbon, and desaturation and cleavage of C‐C bonds, that are likely to be initiated by ferryl complexes in other NH‐Fe enzymes. Recent successes in explaining and exploiting this potent and versatile enzymatic strategy will be highlighted.