Redox Chemistry and Biology of Thiols
- 1st Edition - May 25, 2022
- Imprint: Academic Press
- Editors: Beatriz Alvarez, Marcelo Comini, Gustavo Salinas, Madia Trujillo
- Language: English
- Paperback ISBN:9 7 8 - 0 - 3 2 3 - 9 0 2 1 9 - 9
- eBook ISBN:9 7 8 - 0 - 3 2 3 - 9 1 5 6 6 - 3
Redox Chemistry and Biology of Thiols offers an applied, comprehensive overview of redox chemistry and biology of thiol-dependent processes. Running from basic biology and chemi… Read more
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Request a sales quoteRedox Chemistry and Biology of Thiols offers an applied, comprehensive overview of redox chemistry and biology of thiol-dependent processes. Running from basic biology and chemistry of redox phenomena to research methods and highlighting recently identified roles of thiols across cellular and bodily systems, this book draws upon a range of disciplines to illuminate new research directions, new applications of thiol studies, and clinical translation. Sections cover thiol oxidizing species, thiol reactivity and modifications, thioredoxin, glutaredoxin, glutathione, peroxidases, thiol repair enzymes, thiol oxidative signaling, disulfide bond formation, thiol-based redox biosensors, cysteine and hydrogen sulfide metabolism, iron-sulfur cluster biogenesis, thiols in chloroplasts, blood thiols, sugar and polyamine thiols in pathogenic organisms, redox medicine (therapeutic applications of thiols and drug development), as well as methods and bioinformatics tools.
- Runs from basic thiol biology and chemistry to applications and clinical translation
- Provides methods and protocols that will power new research across biomedicine, cell biology, plant biology, drug development, and protein folding and modulation
- Includes chapter contributions from international leaders in the field
Life science researchers in biochemistry, molecular biology, and cell biology; clinical chemists and pharmaceutical scientists; and medical and analytical chemists Clinicians and students
- Cover image
- Title page
- Table of Contents
- Copyright
- Cover Credit
- Contributors
- Preface
- Acknowledgments
- Chapter 1: Basic concepts of thiol chemistry and biology
- Abstract
- Acknowledgments
- 1: Thiols in biology
- 2: The thiol group confers unique properties to the amino acid cysteine
- 3: Thiols ionize to thiolates
- 4: Thiolates are excellent nucleophiles
- 5: Thiols can be oxidized
- 6: Redox versatility of thiols
- 7: The thiol-disulfide exchange reaction can be catalyzed by proteins of the thioredoxin superfamily
- 8: The thioredoxin and the glutahione-glutaredoxin systems: Pathways that use the thiol-disulfide exchange reaction as a leitmotiv
- 9: The concentrations of thiols and oxidized derivatives are under kinetic control
- 10: Cys diversity in proteins
- 11: Concluding remarks
- References
- Chapter 2: Chemical basis of cysteine reactivity and specificity: Acidity and nucleophilicity
- Abstract
- Acknowledgments
- 1: Measuring pKa
- 2: On the “conservation” of pKa values
- 3: Acidic cysteines and catalytic cysteines, is there a connection?
- 4: What can we learn from the pKa of a protein cysteine? pH and species distribution
- 5: Nucleophilicity
- 6: Nucleophilic catalysis
- 7: Concluding remarks
- References
- Chapter 3: Computational functional analysis of cysteine residues in proteins
- Abstract
- 1: Introduction
- 2: Computational methods
- 3: Remarks and conclusions
- References
- Chapter 4: Global approaches for protein thiol redox state detection and quantification
- Abstract
- Acknowledgments
- 1: Introduction
- 2: The chemistry of thiols
- 3: Exploiting thiol chemistry to detect and quantify oxidative thiol modifications
- 4: Differential thiol labeling in MS-based redox proteomics
- 5: General considerations
- 6: Experimental pitfalls
- 7: What to expect from the results
- 8: How to evaluate and interpret the results
- 9: Conclusions
- References
- Chapter 5: Thiol oxidation by biologically-relevant reactive species
- Abstract
- Acknowledgments
- 1: Introduction
- 2: Biologically relevant thiol oxidants
- 3: One-electron thiol oxidants
- 4: Two-electron thiol oxidants
- 5: Conclusions and perspectives
- References
- Chapter 6: Thiyl radicals: Formation, properties, and detection
- Abstract
- 1: Introduction
- 2: Formation
- 3: Properties
- 4: Detection
- 5: Conclusions
- References
- Chapter 7: Detection of the oxidation products of thiols: Disulfides, and sulfenic, sulfinic, and sulfonic acids
- Abstract
- 1: Introduction
- 2: Activity-based detection of cysteine modifications
- 3: Indirect profiling of cysteine oxidation
- 4: Reaction-based profiling of cysteine OxiPTMs with chemoselective probes
- 5: Profiling of protein sulfonic acids (–SO3H)
- 6: Conclusions and outlook
- References
- Chapter 8: Biochemistry and detection of S-nitrosothiols
- Abstract
- Acknowledgments
- 1: Introduction
- 2: Formation of RSNO
- 3: Other important reactions of RSNO
- 4: Detection of RSNO
- 5: RSNO in physiology
- 6: Concluding remarks
- References
- Chapter 9: Thiol modification and signaling by biological electrophiles
- Abstract
- 1: Introduction
- 2: Biological electrophiles
- 3: Determinants and modulators of electrophilic signaling
- 4: Summary
- References
- Chapter 10: Thioredoxin and glutathione reductases
- Abstract
- Acknowledgments
- 1: Thioredoxin reductases and glutathione reductases—The simple picture
- 2: Thioredoxin reductases and glutathione reductases—Redundancy and higher complexity
- 3: Inhibition of thioredoxin reductases for therapeutic purposes
- 4: Concluding remarks—Biological and medical importance of thioredoxin reductases and glutathione reductases
- References
- Chapter 11: Functional plasticity in the thioredoxin family: FeS-thio- and glutaredoxins
- Abstract
- 1: Redox signaling and the thioredoxin family of protein redoxins
- 2: FeS-redoxins
- 3: Concluding remarks
- References
- Chapter 12: Glutathione and glutathione-dependent enzymes
- Abstract
- Acknowledgments
- 1: Glutathione properties, concentrations, and ideologies
- 2: De novo synthesis, regeneration, and degradation of glutathione
- 3: Physiological functions of glutathione
- 4: Conclusion
- References
- Chapter 13: Thiol- and selenol-based peroxidases: Structure and catalytic properties
- Abstract
- Acknowledgments
- 1: Introduction
- 2: Peroxiredoxins
- 3: Glutathione peroxidases
- 4: Organic hydroperoxide resistance protein (Ohr)/osmotically inducible protein C (OsmC)
- 5: Final remarks
- References
- Chapter 14: Thiol peroxidase-based redox relays
- Abstract
- 1: The conundrum of selective and efficient protein thiol oxidation
- 2: Thiol peroxidase-based redox relays
- 3: The Prx2-STAT3 redox relay paradigm
- 4: Conclusion
- References
- Chapter 15: Compartmentalized disulfide bond formation pathways
- Abstract
- 1: Disulfide bonds
- 2: Principles of disulfide bond formation during oxidative protein folding
- 3: Disulfide bond formation in the ER
- 4: Disulfide bond formation in the IMS
- 5: Reducing pathways in the ER
- 6: Reducing pathways in the IMS
- 7: Conclusions
- References
- Chapter 16: Disulfide bond formation in Escherichia coli
- Abstract
- 1: Disulfide bond formation and oxidative folding
- 2: The Escherichia coli Dsb system
- 3: Diversity of disulfide bond formation pathways in bacteria
- 4: Engineering Escherichia coli for disulfide bond formation
- 5: Disulfide-bond engineering for protein stability
- 6: Future perspectives for Dsb system research
- References
- Chapter 17: Thiol-based redox probes
- Abstract
- 1: Introduction
- 2: Fundamental principles of genetically encoded redox sensors
- 3: Probes for monitoring small molecule thiols
- 4: Probes for monitoring peroxides
- 5: Probes for other thiol species
- 6: Probes for monitoring redox enzyme activity
- 7: Which probe should I use?
- 8: What remains to be done?
- References
- Further reading
- Chapter 18: Selenocysteine-containing proteins
- Abstract
- Acknowledgments
- 1: Selenocysteine, the 21st amino acid
- 2: The selenocysteine pathway
- 3: Why selenocysteine?
- 4: Families of selenoproteins
- 5: Evolution of selenocysteine
- 6: Concluding remarks
- References
- Chapter 19: Overview of cysteine metabolism
- Abstract
- 1: Sources of cysteine
- 2: Cysteine catabolism
- 3: Cysteine posttranslational modifications
- References
- Chapter 20: Hydrogen sulfide and persulfides
- Abstract
- 1: Hydrogen sulfide and persulfides: Long-lost thiol relatives
- 2: Biological formation of H2S
- 3: Biologically relevant physical and chemical properties of H2S
- 4: In vivo decay of H2S
- 5: H2S quantification methods
- 6: Persulfides as potential transducers of H2S signaling
- 7: Pathways for persulfide formation
- 8: The unique chemistry of persulfides
- 9: Detection of protein persulfides
- 10: Final considerations on H2S signaling
- References
- Chapter 21: The role of thiols in iron–sulfur cluster biogenesis
- Abstract
- Acknowledgments
- 1: Introduction
- 2: A basic blueprint for Fe-S cluster biogenesis
- 3: The GSH-binding transporter Atm1 exports sulfur intermediates for cytosolic Fe-S cluster biogenesis, iron regulation, and tRNA thiolation pathways
- 4: Fe-S cluster biogenesis in the cytosolic/nuclear compartment of eukaryotes
- 5: CGFS Grxs serve as hubs for cytosolic Fe-S cluster trafficking and iron regulation pathways
- 6: Alternative LMW thiols are implicated in Fe-S cluster biogenesis pathways
- 7: Summary and conclusions
- References
- Chapter 22: Thiol-based redox control in chloroplasts
- Abstract
- 1: Introduction
- 2: Control of redox homeostasis in chloroplasts by thiol-based systems
- 3: Redox regulation of the chloroplastic metabolism
- 4: Protein oxidation in response to day-night transition
- 5: Conclusions
- References
- Chapter 23: Sugar-based cysteine thiols recruited for oxidative stress defense and redox regulation
- Abstract
- 1: Introduction
- 2: Biosynthesis of sugar-based LMW thiols
- 3: Biophysical and biochemical properties of mycothiol and bacillithiol
- 4: Protective roles of BSH and MSH
- 5: Posttranslational modification by sugar-based LMW thiols—The S-thiolomes
- 6: From enzymes to tools: Mrx- and Brx-based biosensors to dynamically visualize MSH/MSSM and BSH/BSSB changes in bacteria
- 7: Conclusion
- References
- Chapter 24: Polyamine-based thiols in pathogens
- Abstract
- Acknowledgments
- 1: Polyamine-based thiols and oddities of nature
- 2: “To adapt or not to adapt?” this was the question for the thiol-redox systems
- 3: Thiol-dependent redox pathways in trypanosomatids
- 4: Monoglutathionylspermidine in Proteobacteria
- 5: Concluding remarks
- References
- Chapter 25: Thiols in blood
- Abstract
- 1: Blood
- 2: Blood as a source and a sink of oxidants
- 3: Thiols in blood cells
- 4: Thiols in plasma
- 5: Crosstalk between plasma and blood cell thiols
- 6: Overall picture of thiols in blood
- References
- Chapter 26: A thiol chemistry perspective on redox medicine
- Abstract
- 1: Endogenous protein and low molecular weight thiols
- 2: Thiols in cellular and organism redox communication
- 3: Thiol therapeutics: Drugs and protein targets
- 4: Analysis of redox modifications at thiols and other sulfur compounds
- 5: Redox systems biology: Bioinformatics and computational approaches
- References
- Chapter 27: Therapeutic applications of low-molecular-weight thiols and selenocompounds
- Abstract
- Acknowledgments
- 1: Introduction
- 2: Selenium vs sulfur: The chemical point of view
- 3: The limitations of LMW-Se as mimics of Selenoproteins
- 4: Organoselenium molecules: Focus on Ebselen, Ethaselen, and Diphenyl diselenide
- 5: Modulation of KEAP1-NRF2 by Organoselenium molecules
- 6: Therapeutic use of LMW-SH
- 7: Conclusions
- References
- Chapter 28: Thiol targets in drug development to combat bacterial infections
- Abstract
- Acknowledgments
- 1: Introduction
- 2: Thiol targets in the development of antimicrobial compounds
- 3: Conclusion
- References
- Index
- Edition: 1
- Published: May 25, 2022
- Imprint: Academic Press
- No. of pages: 746
- Language: English
- Paperback ISBN: 9780323902199
- eBook ISBN: 9780323915663
BA
Beatriz Alvarez
Dr. Beatriz Alvarez is a Professor at the Laboratory of Enzymology, School of Sciences, Universidad de la República, Montevideo, Uruguay. Her research interests span the areas of redox biochemistry, kinetics and enzymology, especially in relation to biological thiols and hydrogen sulfide.
Affiliations and expertise
Professor, Laboratory of Enzymology, School of Sciences, Universidad de la República, Montevideo, UruguayMC
Marcelo Comini
Dr. Marcelo Comini is a Principal Investigator at the Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo, Uruguay. He is a Biochemist (Universidad Nacional del Litoral, Argentina) and Dr. rer. nat. from the Technische Universität Brausnchweig (Germany). The research interest of his lab encompasses understanding the role of different components of the thiol-redox system of trypanosomatids, the identification of inhibitors thereof, and the development of fluorescent-protein redox biosensors.
Affiliations and expertise
Principal Investigator, Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo, UruguayGS
Gustavo Salinas
Dr. Gustavo Salinas is a Principal Investigator at the Worm Biology Laboratory, Institut Pasteur de Montevideo, Uruguay, as well as a Professor at the Department of Biosciences, School of Chemistry, Universidad de la República, Uruguay. His research contributes to the understanding of linked thioredoxin-glutathione systems in parasites, glutathione-independent deglutathionylation, selenocysteine horizontal gene transfer and the use of selenocysteine in fungi. He is also interested in anaerobic mitochondria and recently discovered key steps in the biosynthesis of rhodoquinone, an electron transporter used in anaerobic bioenergetics.
Affiliations and expertise
Principal Investigator, Worm Biology Laboratory, Institut Pasteur de Montevideo; Professor, Department of Biosciences, School of Chemistry, Universidad de la República, UruguayMT
Madia Trujillo
Madia Trujillo, MD, PhD, is an Associate Professor of Biochemistry at the School of Medicine and an Investigator at the Centro de Investigaciones Biomédicas, Universidad de la República, Uruguay. Her research focuses on the characterization of the reactions of biologically relevant oxidants as well as in the mechanisms of their sensing and detoxification, particularly in humans and human pathogens.
Affiliations and expertise
Associate Professor, Biochemistry, School of Medicine; Investigator, Centro de Investigaciones Biomédicas, Universidad de la República, UruguayRead Redox Chemistry and Biology of Thiols on ScienceDirect