Anaerobic bacterial response to nitric oxide stress: Widespread misconceptions and physiologically relevant responses

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Abstract

How anaerobic bacteria protect themselves against nitric oxide-induced stress is controversial, not least because far higher levels of stress were used in the experiments on which most of the literature is based than bacteria experience in their natural environments. This results in chemical damage to enzymes that inactivates their physiological function. This review illustrates how transcription control mechanisms reveal physiological roles of the encoded gene products. Evidence that the hybrid cluster protein, Hcp, is a major high affinity NO reductase in anaerobic bacteria is reviewed: if so, its trans-nitrosation activity is a nonspecific secondary consequence of chemical inactivation. Whether the flavorubredoxin, NorV, is equally effective at such low [NO] is unknown. YtfE is proposed to be an enzyme rather than a source of iron for the repair of iron-sulfur proteins damaged by nitrosative stress. Any reaction catalyzed by YtfE needs to be revealed. The concentration of NO that accumulates in the cytoplasm of anaerobic bacteria is unknown, but indirect evidence indicates that it is in the pM to low nM range. Also unknown are the functions of the NO-inducible cytoplasmic proteins YgbA, YeaR, or YoaG. Experiments to resolve some of these questions are proposed.

Original languageEnglish
JournalMolecular Microbiology
Early online date11 Mar 2021
DOIs
Publication statusE-pub ahead of print - 11 Mar 2021

Bibliographical note

© 2021 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.

Keywords

  • chemical damage
  • enzymic activity of YtfE
  • hybrid cluster protein
  • nitrosative stress
  • non-physiological artefacts

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