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

ABSTRACT: Fe_BMbs 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_BMb1 proteins loaded with Fe^II, Co^II, or Zn^II metal ions at the Fe_B site (Fe^II/Co^II/Zn^II-Fe_BMb1(MF-heme)). FTIR detection of the ν(NNO) band of N₂O 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_BMb1

SUBMITTER: Sabuncu S 

PROVIDER: S-EPMC6470035 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature