Protein Sensors and Reactive Oxygen Species, Part B: Thiol Enzymes and Proteins

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Helmut Sies, Lester Packer
Academic Press, Mar 8, 2002 - Science - 404 pages
This volume of Methods in Enzymology is a companion to Volume 347 and addresses direct sensing of reactive oxygen species and related free radicals by thiol enzymes and proteins.

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Chapter 1 Thiols in Redox Mechanism of Ribonucleotide Reductase
Chapter 2 Tyrosyl Radicals and Ribonucleotide Reductase
Chapter 3 FlavinDependent Sulfhydryl Oxidases in Protein Disulfide Bond Formation
Chapter 4 Analyzing Cotranslational Protein Folding and Disulfide Formation by Diagonal Sodium Dodecyl SulfatePolyacrylamide Gel Electrophoresis
Chapter 5 Disulfide Reduction in Major Histocompatibility Complex Class IIRestricted Antigen Processing by InterferonγInducible Lysosomal Thiol ...
Chapter 6 Thiol Oxidation and Reduction in Major Histocompatibility Complex Class IRestricted Antigen Processing and Presentation
Chapter 7 Disulfide Bond Formation in Periplasm Escherichia coli
Chapter 8 Protein Disulfide Isomerase as an Enzyme and a Chaperone in Protein Folding
Chapter 20 Gene Expression and Thiol Redox State
Chapter 21 Redox Flow as an Instrument of Gene Regulation
Chapter 22 Optical Methods for Measuring Zinc Binding and Release Zinc Coordination Environments in Zinc Finger Proteins and Redox Sensitivity...
Chapter 23 Metallothionein Expression and Oxidative Stress in the Brain
Chapter 24 Reversible Oxidation of HIV2 Protease
Chapter 25 Thiol Enzymes Protecting Mitochondria against Oxidative Damage
DithiolDisulfide Equilibrium in Serine Threonine Phosphatase Calcineurin
Chapter 27 Glutathione Reductase from Bovine Brain

Chapter 9 Characterization of RedoxActive Proteins on Cell Surface
Chapter 10 Measurement of Reduction of Disulfide Bonds in Plasmin by Phosphoglycerate Kinase
Assay and Biological Significance
Chapter 12 Role of Yeast FlavinContaining Monooxygenase in Maintenance of ThiolDisulfide Redox Potential
Chapter 13 Identification of Cysteine Sulfenic Acid in AhpC of Alkyl Hydroperoxide Reductase
Chapter 14 Glutaredoxins and Oxidative Stress Defense in Yeast
Chapter 15 Quantitation of Protein Sulfinic and Sulfonic Acid Irreversibly Oxidized Protein Cysteine Sites in Cellular Proteins
Chapter 16 cJun Regulation by SGlutathionylation
Role of Thiol Oxidation and Catalysis by Glutaredoxin
Chapter 18 Roles of Nrf2 in Activation of Antioxidant Enzyme Genes via Antioxidant Responsive Elements
Chapter 19 Enzymatic Pathways of β Elimination of Chemopreventive Selenocysteine Se Conjugates
Chapter 28 RedoxMediated Functional and Structural Changes in Insulin Receptor Kinase
Detecting Sulfenic Acid Intermediates and Examining Reversible Inactivation
Chapter 30 Protein CrossLinking by SelfAssisted Intermolecular Disulfide Bond Formation
Chapter 31 Sulfhydryl Oxidases as Factors for Mitochondrial Biogenesis
Chapter 32 Activation of Iron Regulatory Protein1 by Oxidative Stress
Chapter 33 Mouse Astrocyte Cultures Used to Study Antioxidant Property of Metallothionein Isoforms
Chapter 34 Model Peptide Substrates and Ligands in Analysis of Action of Mammalian Protein DisulfideIsomerase
SensorTransducer of Oxidative Stress and Nitric Oxide
Author Index
Subject Index

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About the author (2002)

Helmut Sies is an Honorary Member of the American Society for Biochemistry and Molecular Biology. He received an Honorary Ph.D. from the University of Buenos Aires, Argentina in 1996. Dr. Sies is a member of the Northrhine-Westphalian Academy of Sciences, Germany, and a Corresponding Member of both the Academy of Sciences of Heidelberg, Germany, and the Academy of Medicine, Buenos Aires, Argentina. He has received many awards and prizes, including the FEBS Anniversary Prize awarded by the Federation of European Biochemical Societies, 1978; the Distinguished Foreign Scholar award, MASUA, 1985; the Silver Medal, Karolinska Institute, Stockholm, 1986; the Ernst Jung Preis fur Medizin, 1988; the Claudius-Galenus-Preis, 1990; and the ISFE-Preis, 1994. Dr. Sies sereves on the editorial board and advisory committee for twelve journals, has edited numerous books, and has published more than 400 original articles and chapters. He received his M.D. at the University of Munich in 1967 and currently serves as Full Professor and Chairman of the Department of Physiological Chemistry at the University of D sseldorf.

Lester Packer received a PhD in Microbiology and Biochemistry in 1956 from Yale University. In 1961, he joined the University of California at Berkeley serving as Professor of Cell and Molecular Biology until 2000, and then was appointed Adjunct Professor, Pharmacology and Pharmaceutical Sciences, School of Pharmacy at the University of Southern California.

Dr Packer received numerous distinctions including three honorary doctoral degrees, several distinguished Professor appointments. He was awarded Chevalier de l'Ordre National du Merite (Knight of the French National Order of Merit) and later promoted to the rank of Officier. He served as President of the Society for Free Radical Research International (SFRRI), founder and Honorary President of the Oxygen Club of California.

He has edited numerous books and published research; some of the most cited articles have become classics in the field of free radical biology:

Dr Packer is a member of many professional societies and editorial boards. His research elucidated - the Antioxidant Network concept. Exogenous lipoic acid was discovered to be one of the most potent natural antioxidants and placed as the ultimate reductant or in the pecking order of the "Antioxidant Network" regenerating vitamins C and E and stimulating glutathione synthesis, thereby improving the overall cellular antioxidant defense. The Antioxidant Network is a concept addressing the cell's redox status. He established a world-wide network of research programs by supporting and co-organizing conferences on free radical research and redox biology in Asia, Europe, and America.

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