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Application of Genetically Encoded Fluorescent Nitric Oxide (NO•) Probes, the geNOps, for Real-time Imaging of NO• Signals in Single Cells
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Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and

Chelsey R Fontenot1, Zishuo Cheng1, Huangen Ding1

  • 1Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, United States.

Frontiers in Molecular Biosciences
|September 26, 2022
PubMed

Insights

Mitochondrial protein mitoNEET binds nitric oxide (NO) to its iron-sulfur cluster, inhibiting redox activity. Light can reverse this, suggesting NO regulates mitoNEET

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Metabolism

Background:

  • MitoNEET is a mitochondrial outer membrane protein involved in energy metabolism and cellular redox balance.
  • Dysregulation of mitoNEET is implicated in type II diabetes, neurodegenerative diseases, and cancer.
  • The protein features a redox-active [2Fe-2S] cluster in its cytosolic domain.

Purpose of the Study:

  • To investigate the interaction between nitric oxide (NO) and the [2Fe-2S] cluster of mitoNEET.
  • To determine if NO binding affects the cluster's redox activity and stability.
  • To explore the potential regulatory role of NO in mitoNEET function.

Main Methods:

  • Biochemical characterization of the reduced [2Fe-2S] cluster in mitoNEET (mitoNEET45-108).
  • Spectroscopic analysis to study NO binding to the cluster.
  • Assessment of cluster redox transitions and stability upon NO binding and light exposure.

Main Results:

  • The reduced [2Fe-2S] cluster of mitoNEET45-108 binds nitric oxide (NO) without structural disruption.
  • NO binding inhibits the redox transition of the [2Fe-2S] cluster.
  • Light excitation dissociates NO, restoring the cluster's redox activity.

Conclusions:

  • Nitric oxide (NO) reversibly binds to the reduced [2Fe-2S] cluster of mitoNEET.
  • This binding modulates the cluster's redox activity, suggesting a regulatory mechanism.
  • NO may control mitoNEET's electron transfer function in the mitochondrial outer membrane.
Keywords:
electron transfer (ET)iron-sulfurmitochondianitric oxideoxidation reduction

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