Nitric Oxide Reductase Activity in Heme-Nonheme Binuclear Engineered Myoglobins through a One-Electron Reduction Cycle

Sinan Sabuncu, Julian H. Reed, Yi Lu, Pierre Moënne-Loccoz

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Fe B Mbs are structural and functional models of native bacterial nitric oxide reductases (NORs) generated through engineering of myoglobin. These biosynthetic models replicate the heme-nonheme diiron site of NORs and allow substitutions of metal centers and heme cofactors. Here, we provide evidence for multiple NOR turnover in monoformyl-heme-containing Fe B Mb1 proteins loaded with Fe II , Co II , or Zn II metal ions at the Fe B site (Fe II /Co II /Zn II -Fe B Mb1(MF-heme)). FTIR detection of the (NNO) band of N 2 O at 2231 cm -1 provides a direct quantitative measurement of the product in solution. A maximum number of turnover is observed with Fe II -Fe B Mb1(MF-heme), but the NOR activity is retained when the Fe B site is loaded with Zn II . These data support the viability of a one-electron semireduced pathway for the reduction of NO at binuclear centers in reducing conditions.

Original languageEnglish (US)
Pages (from-to)17389-17393
Number of pages5
JournalJournal of the American Chemical Society
Volume140
Issue number50
DOIs
StatePublished - Dec 19 2018

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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