Abstract
(4-Hydroxyphenyl)pyruvate dioxygenase (HPPD) is an unusual alpha-keto acid-dependent non-heme iron dioxygenase as it incorporates both atoms of dioxygen into a single substrate, paralleling the extradiol dioxygenases. CD/MCD studies of the catalytically active ferrous site and its interaction with substrate reveal a geometic and electronic structure and mechanistic approach to oxygen activation which bridges those of the alpha-KG-dependent and the extradiol dioxygenases.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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4-Hydroxyphenylpyruvate Dioxygenase / chemistry*
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4-Hydroxyphenylpyruvate Dioxygenase / metabolism
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Binding Sites
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Circular Dichroism / methods
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Ferrous Compounds / chemistry*
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Ferrous Compounds / metabolism
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Ketoglutaric Acids / chemistry*
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Ketoglutaric Acids / metabolism
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Oxygen / chemistry*
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Oxygen / metabolism
Substances
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Ferrous Compounds
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Ketoglutaric Acids
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4-Hydroxyphenylpyruvate Dioxygenase
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Oxygen