Narrow Results

The experimental and computational study of bacterial thioredoxin, an E. coli protein, at THz frequencies is presented. The absorption spectrum of the entire protein in water was studied numerically in the terahertz range (0.1 – 2 THz). In our work, the initial X-ray molecular structure of thioredoxin was optimized using the molecular dynamical (MD) simulations at room temperature and atmospheric pressure. The effect of a liquid content of a bacterial cell was taken into account explicitly via the simulation of water molecules using the TIP3P water model. Using atomic trajectories from the room-temperature MD simulations, thioredoxin's THz vibrational spectrum and the absorption coefficient were calculated in a quasi harmonic approximation.

For our terahertz transmission measurements, we used solutions of thioredoxin in distilled water obtained from Sigma. The experimental and simulated signatures are correlated and dominant peaks are close in frequencies. The results of this study demonstrate that terahertz spectroscopy is a promising tool in generating spectral data for cellular components of bio agents such as bacterial cells and spores.

The following sections are included:

• Summary

• Introduction and Historical Perspective

• The Thioredoxin System
  • Thioredoxin Reductase and Selenium
  • Structure of Mammalian Thioredoxin Reductase
  • Mechanism of Mammalian Thioredoxin Reductase

• The Glutaredoxin System

• Redox Regulation of Cellular Function

• Future Perspectives

• Acknowledgments

• References

The following sections are included:

• Summary

• Ferredoxin-Thioredoxin system
  • NADP/Thioredoxin System

• Applications of Thioredoxin
  • Alleviation of Allergies
  • Improved Dough Quality

• Thioredoxin-Enriched Grain
  • Cereal Transformations
  • Properties of Transgenic Cereals

• A New Development

• Note added in Proof

• References

The following sections are included:

• Summary

• Cytoprotective Effects of Thioredoxin

• Thioredoxin and its Related Molecules

• Thioredoxin Knock Out and Transgenic Mice

• Characteristic of Trx-Tg Mice
  • Resistance Against Focal Cerebral Ischemic Injury⁸
  • Resistance Against Excitotoxic Hippocampal Injury⁹
  • Resistance Against Oxidative Stress and Elongated Survival
  • Pancreatic Beta Cell Specific Overexpression of Thioredoxin⁴⁴

• Extracellular Function of Thioredoxin

• A Truncated Form of Thioredoxin

• Chemokine-Like Activity of Thioredoxin

• Circulating Thioredoxin Levels in Human Plasma

• Thioredoxin Binding Proteins

• Redox Regulation of Transcription Factors by Thioredoxin

• Redox Regulation of Apoptosis by Thioredoxin

• Conclusion

• Ackonwledgments

• References

The following sections are included:

• Summary

• Disulfides and Protein Structure and Stability

• Quality Control in the Endoplasmic Reticulum
  • General Quality Control and Secretion
  • Formation of Disulfides in the Endoplasmic Reticulum
  • Constraints Imposed by the Folding Environment of the ER

• Oxidative Protein Folding

• Protein Disulfide Isomerase
  • Structural Organization — The Thioreoxin Family
  • Active Site Properties
  • Catalytic Properties of PDI and its Mutants

• Redox Optimum for Oxidative Folding
  • Redox Dependence of PDI
  • Redox Potential of Substrates

• Mechanism of Isomerization
  • Scanning and Escape

• Substrate Inhibition and Recycling of Oxidized PDI
  • Substrate Inhibition

• Secretion in Yeast
  • Redox and Structural Requirements for Yeast Growth

• References

The following sections are included:

• Summary
  • Introduction

• OxyR
  • Identification of OxyR and Its Target Genes
  • OxyR Activation by Disulfide Bond Formation Between C199 and C208
  • OxyR Reduction by Glutaredoxin
  • Structure of the OxyR Regulatory Domain

• σ^R and RsrA
  • Identification of σ^R and RsrA and Their Target Genes
  • Release of σ^R Upon Disulfide Bond Formation in RsrA
  • RsrA Reduction by Thioredoxin

• Yap1
  • Identification of Yap1p and its Target Genes
  • Block of Yap1p Nuclear Export by Disulfide Bond Formation
  • Regulation of Yap1p Activity by Thioredoxin

• Concluding Remarks

• Acknowledgments

• References

The following sections are included:

• Summary

• Introduction

• TRX and Its Related Molecules

• TRX Binding Proteins

• Redox Regulation of Transcription Factors by TRX

• Redox Regulation of Apoptosis by TRX

• Cytoprotective Effects of TRX

• Aging and TRX Overexpressing Transgenic Mice

• Oxidative Stress and Central Nervous System

• Conclusion

• References

The following sections are included:

• Introduction

• The Thioredoxin System

• The Glutaredoxin System

• Redox Regulation by Thioredoxin and Glutaredoxin

• Effects of Oxidants and Antioxidants

• Future Perspectives

• Acknowledgments

• References

The experimental and computational study of bacterial thioredoxin, an E. coli protein, at THz frequencies is presented. The absorption spectrum of the entire protein in water was studied numerically in the terahertz range (0.1 – 2 THz). In our work, the initial X-ray molecular structure of thioredoxin was optimized using the molecular dynamical (MD) simulations at room temperature and atmospheric pressure. The effect of a liquid content of a bacterial cell was taken into account explicitly via the simulation of water molecules using the TIP3P water model. Using atomic trajectories from the room-temperature MD simulations, thioredoxin's THz vibrational spectrum and the absorption coefficient were calculated in a quasi harmonic approximation.

For our terahertz transmission measurements, we used solutions of thioredoxin in distilled water obtained from Sigma. The experimental and simulated signatures are correlated and dominant peaks are close in frequencies. The results of this study demonstrate that terahertz spectroscopy is a promising tool in generating spectral data for cellular components of bio agents such as bacterial cells and spores.