Report

Active site rearrangement and structural divergence in prokaryotic respiratory oxidases

See allHide authors and affiliations

Science  04 Oct 2019:
Vol. 366, Issue 6461, pp. 100-104
DOI: 10.1126/science.aay0967

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Hemes switch spots in a terminal oxidase

Reduction of molecular oxygen to water is the driving force for respiration in aerobic organisms and is catalyzed by several distinct integral membrane complexes. These include an exclusively prokaryotic enzyme, cytochrome bd–type quinol oxidase, which is a potential antimicrobial target. Safarian et al. determined a high-resolution cryo–electron microscopy structure of this enzyme from the enteric bacterium Escherichia coli. Comparison to a homolog reveals a complete relocation of the site of oxygen binding and reduction caused by a change in the arrangement of heme cofactors and channels in the protein scaffold. This switch illustrates the diversity of structure and function in this family of enzymes and might reflect different biochemical roles of these homologs.

Science, this issue p. 100

View Full Text