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Efficient Sampling of Genetically Encoded Biosensor Design Space Enabled with a Design of Experiments and Automation Workflow
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Characterization of a globin-coupled oxygen sensor with a gene-regulating function.

Liesbet Thijs1, Evi Vinck, Alessandro Bolli

  • 1Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, B-2610, Antwerp, Belgium.

The Journal of Biological Chemistry
|October 11, 2007
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Summary

Azotobacter vinelandii globin-coupled sensors (GCSs) bind oxygen with high affinity. AvGReg178 and AvGReg exhibit distinct heme coordination and O(2) binding kinetics, with AvGReg178 potentially involved in NO detoxification.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Globin-coupled sensors (GCSs) are multi-domain proteins found in Archaea and bacteria.
  • GCSs are believed to sense gaseous ligands like O(2) and transduce signals via conformational changes.
  • The Azotobacter vinelandii GCS, AvGReg, comprises a heme-binding domain (AvGReg178) and a transducer domain.

Purpose of the Study:

  • To clone, express, and purify the AvGReg178 heme-binding domain and the full AvGReg protein from Azotobacter vinelandii.
  • To characterize the heme-binding properties, O(2) affinity, and ligand-binding kinetics of AvGReg178 and AvGReg.
  • To investigate the potential role of AvGReg178 in oxygen-mediated nitric oxide detoxification.

Main Methods:

  • Cloning, expression, and purification of AvGReg178 and AvGReg proteins.
  • Spectroscopic analysis to determine heme iron coordination in different states (oxygenated, deoxygenated).
  • Oxygen binding isotherms and carbon monoxide binding kinetics measurements.

Main Results:

  • Purified AvGReg178 binds O(2) and forms a stable oxy-heme complex.
  • Ferric AvGReg predominantly exhibits bis-histidine heme coordination, while AvGReg178 shows penta-coordinate heme in its deoxygenated ferrous state.
  • AvGReg178 and AvGReg display high O(2) affinity (P(50) values of 0.04 and 0.15 torr at 20°C).
  • AvGReg178 carbonylation is monophasic, similar to myoglobin; AvGReg carbonylation is three-phasic, characteristic of bis-histidine heme proteins.
  • In vitro data suggest AvGReg178 may detoxify nitric oxide (NO) via O(2) mediation, producing metAvGReg178 and nitrate.

Conclusions:

  • AvGReg178 and AvGReg are functional GCSs with high oxygen affinity.
  • Distinct heme coordination and ligand-binding kinetics differentiate the heme-binding domain from the full protein.
  • AvGReg178 shows potential for a dual role in oxygen sensing and nitric oxide detoxification.