The NADPH oxidase (NOX) protein family plays a major role in the physiology of eukaryotes by producing reactive oxygen species. Evolutionarily distant NOXs have been identified in bacterial species including Streptococcus pneumoniae. Although structurally simpler than eukaryotic counterparts, NOX from S. pneumoniae (SpNOX) shows a number of conserved characteristics, allowing it to serve as a model system. Structural, biochemical and mutagenic studies of SpNOX inform our understanding of the NOX protein family. Here, we provide a comparative analysis of bacterial and eukaryotic NOX structure. We discuss the relevant studies in the context of the major questions in NOX structure and function, including the determinants of substrate specificity and the mechanism of activation, electron transfer and hydride transfer.

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Structural and Biochemical Investigation of a Bacterial NOX from Streptococcus pneumoniae

  • Victor R. A. Dubach,
  • Pablo San Segundo-Acosta,
  • Bonnie J. Murphy

摘要

The NADPH oxidase (NOX) protein family plays a major role in the physiology of eukaryotes by producing reactive oxygen species. Evolutionarily distant NOXs have been identified in bacterial species including Streptococcus pneumoniae. Although structurally simpler than eukaryotic counterparts, NOX from S. pneumoniae (SpNOX) shows a number of conserved characteristics, allowing it to serve as a model system. Structural, biochemical and mutagenic studies of SpNOX inform our understanding of the NOX protein family. Here, we provide a comparative analysis of bacterial and eukaryotic NOX structure. We discuss the relevant studies in the context of the major questions in NOX structure and function, including the determinants of substrate specificity and the mechanism of activation, electron transfer and hydride transfer.