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Is Nostoc H-NOX a NO sensor or redox switch?
Ah-Lim Tsai1, Vladimir Berka, Faye Martin
1Division of Hematology, Internal Medicine, University of Texas Houston Medical School, Houston, Texas 77030, USA. Ah-lim.tsai@uth.tmc.edu
Nostoc sp. H-NOX, a bacterial heme protein, differs functionally from human sGC despite structural similarities. It exhibits unique NO binding and autoxidation, suggesting roles in redox or NO sensing for cyanobacteria.
Area of Science:
- Biochemistry
- Molecular Biology
- Cyanobacteria Research
Background:
- Nostoc sp. H-NOX (Ns H-NOX) is a heme protein in symbiotic cyanobacteria.
- It shares sequence and structural homology with human soluble guanylyl cyclase (sGC), suggesting a NO sensing role.
Purpose of the Study:
- To investigate the functional differences between Ns H-NOX and sGC.
- To elucidate the NO sensing mechanism of Ns H-NOX.
Main Methods:
- UV-vis spectroscopy
- Electron Paramagnetic Resonance (EPR)
- Near-Infrared Magnetic Circular Dichroism (NIR MCD)
- Ligand binding experiments
Main Results:
- Ns H-NOX shows limited pentacoordinate NO heme formation, unlike sGC.
- Two hexacoordinate NO complexes form in Ns H-NOX, dependent on NO concentration.
- Ferric Ns H-NOX autoxidizes and forms a hexacoordinate complex, indicating conformational changes.
Conclusions:
- Ns H-NOX exhibits distinct NO binding and conformational properties compared to sGC.
- These differences suggest Ns H-NOX may function as a redox or NO sensor in cyanobacteria.
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