Understanding copper-thiolate containing electron transfer centers by incorporation of unnatural amino acids and the Cu A center into the type 1 copper protein azurin

Tiffany D. Wilson, Yang Yu, Yi Lu

Research output: Contribution to journalReview article

Abstract

Highly covalent copper-thiolate bonds are salient features of ubiquitous type 1 (T1) blue copper and purple Cu A electron transfer (ET) centers in proteins. These centers are found in a wide variety of proteins, each having its own electron transfer partners, requiring the centers to possess a broad range of reduction potentials to match those of their redox partners and to perform ET functions under various driving forces, all while maintaining high ET efficiency. Unraveling the secrets of the success realized by these ET centers has relied upon the expertise of many scientific disciplines and sub-disciplines, including inorganic chemistry, microbiology, biochemistry, and biophysical chemistry. Here, we review the contribution of protein engineering approaches-namely, the incorporation of unnatural amino acids and a biosynthetic Cu A cofactor into the T1 copper protein azurin-to advancing the current understanding of how the unique structures of T1 copper and Cu A centers confer their proteins with efficient and tailored ET properties.

Original languageEnglish (US)
Pages (from-to)260-276
Number of pages17
JournalCoordination Chemistry Reviews
Volume257
Issue number1
DOIs
StatePublished - Jan 1 2013

Keywords

  • Biosynthetic chemistry
  • Blue copper
  • Copper proteins
  • Cu
  • Cupredoxins
  • Electron transfer
  • Protein engineering
  • Redox
  • Type 1 copper

ASJC Scopus subject areas

  • Chemistry(all)

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