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March 13, 2026Proceedings of the National Academy of SciencesOpen Access

The Mycobacterium smegmatis bd -II terminal oxidase employs a carboxylate shift mechanism

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Authors

TKTerezia KovalovaStockholm UniversityMJMateusz JanczakStockholm UniversityAGAna P. Gamiz-HernandezStockholm University

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Implication

Biochemical characterization reveals a pH-dependent mechanism for substrate access in Mycobacterium smegmatis, indicating evolutionary insights into bd oxidases.

Key Points

  • This research aims to investigate the mechanisms underlying the function of the bd-II terminal oxidase in Mycobacterium smegmatis.
  • Combined biochemical studies with cryo-electron microscopy (cryo-EM)
  • Overexpressed the appCB operon in native host
  • Conducted multiscale simulations
  • Characterized a highly active bd-II with a k_obs of 30 e- s-1
  • Provided a high-resolution cryo-EM structure at 2.8 Å
  • Identified unique proton pathways and oxygen channels involved in function
  • Proposed that a pH-dependent switch regulates substrate access to the active site

Cite This Study

Kovalova et al. (2026) studied this question.

synapsesocial.com/papers/69b3ab8002a1e69014ccc769https://doi.org/10.1073/pnas.2515348123
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