Structural insights into dioxygen-activating copper enzymes

Amy C. Rosenzweig*, Matthew H. Sazinsky

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

86 Scopus citations

Abstract

Copper-containing enzymes that react with O2 play a key role in many biological processes. Mononuclear, dinuclear and trinuclear copper centers function in O2 binding, activation and subsequent substrate oxidation. Recent advances in the structural biology of O2-activating copper enzymes range from the identification of novel copper centers, such as that of particulate methane monooxygenase, to the elucidation of the details of O2 binding and reactivity in peptidylglycine α-hydroxylating monooxygenase. Structures of phenoxazinone synthase and Fet3 contribute to our understanding of multicopper oxidases. Additionally, details of the tyrosinase structure provide new insight into how dicopper sites confer substrate specificity. A common theme for each of these enzymes is that the protein scaffold plays a major role in dictating the overall function.

Original languageEnglish (US)
Pages (from-to)729-735
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume16
Issue number6
DOIs
StatePublished - Dec 2006

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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