Journal
SCIENCE
Volume 316, Issue 5823, Pages 453-457Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1134697
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Funding
- NIGMS NIH HHS [R01 GM024689-28, R01 GM024689-27, R01 GM024689, R37 GM024689-26, GM24689, R37 GM024689] Funding Source: Medline
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We report the structures of three intermediates in the O-2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O-2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.
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