Abbreviations used
- BSO, L-Buthionine-SR-sulfoximine
- CoQ, Coenzyme Q, ubiquinone
- Eº, E01, ⋯ Reduction potential at nonstandard conditions, standard condition (pH=0), standard conditions (pH=7)
- Ehc, Half-cell reduction potential
- GPx, Glutathione peroxidase
- GR, Glutathione (disulfide) reductase
- Grx(SH)2/GrxSS, Glutaredoxin, glutaredoxin disulfide
- GSH, GSSG, Glutathione, glutathione disulfide
- NAC, N-acetyl-L-cysteine
- NADH, NAD+ Nicotinamide adenine dinucleotide, oxidized form
- NADPH, NADP+, NADP•, Nicotinamide adenine dinucleotide phosphate, oxidized form radical
- ROS, Reactive Oxygen Species
- Reactive Oxygen Species
- SOD, Superoxide dismutase
- Superoxide dismutase
- Trx(SH2)/TrxSS, Thioredoxin, thioredoxin disulfide
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Bücher, T. and M. Klingenberg. 1958. Wege des Wasserstoffs in der lebendigen Organisation. Angew. Chem. 70:552–570.
Schafer, F. Q. and G. R. Buettner. 2000. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30:1191–1212.
Sun, Y. and L. W. Oberley. 1996. Redox regulation of transcriptional activators. Free Radic Biol Med. 21:335–348.
Krebs, H. A. 1967. The redox state of nicotinamide adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Advances in Enzyme Regulation. 5:409–434.
Krebs, H. A. and T. Gascoyne. 1968. The redox state of the nicotinainide-adenine dinucleotides in rat liver homogenates. Biochem. J. 108:513–520.
Krebs, H. A. and R. L. Veech. 1969. Equilibrium relations between pyridine nucleotides and adenine nucleotides and their roles in the regulation of metabolic processes. Advances in Enzyme Regulation. 7:397–413.
Koppenol, W. H. and J. Butler. 1985. Energetics of interconversion reactions of oxyradicals. Adv. Free Radic. Biol. Med. 1:91–131.
Farrington, J. A., M. Ebert, E. J. Land and K. Fletcher. 1973. Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implications for the mode of action of bipyridyl herbicides. Biochim. Biophys. Acta. 314:372–381.
Buettner, G. R. 1993. The pecking order of free radicals and antioxidants: Lipid peroxidation, α-tocopherol, and ascorbate. Arch. Biochem. Biophys., 300:535–543.
Koppenol, W. H. 1997. The chemical reactivity of radicals. In: Free Radical Toxicology (Wallace, K.B., ed.), pp. 3–14, Taylor and Francis, London.
Clark, W. M. ed. 1960. Oxidation-Reduction Potentials of Organic Systems. Williams and Wilkens, Baltimore, MD.
Lardy, H. A. ed. 1949. Respiratory Enzymes. Burgess, Minneapolis, MN.
Burton, K. 1957. Free energydata of biological interest. Ergeb. Physiol. Biol. Chem. Exptl. Pharmakol. 49:275.
Weber, G. 1961. Absorption bands and molar absorption coefficients of substances of biochemical interest. Biochemist’s Handbook. (Long, C. ed.), pp. 81–82, Spon. London.
Cleland, W. W. 1964. Dithiothreitol, a new protective reagent for SH groups. Biochemistry. 3:480–482.
Rodkey, F. L. and J. A. Donovan. 1959. Oxidation-reduction potentials of the diphosphopyridine nucleotide system. J. Biol. Chem. 234:677–680.
Ke, B. 1957. Polarographic behavior of a-lipoic acid. Biochim. Biophys. Acta. 25:650–651.
Aslund, F., K. D. Berndt and A. Holmgren. 1997. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem. 272:30780–30786.
Gilbert, H. F. 1995. Thiol/disulfide exchange equilibria and disulfide bind stability. Methods in Enzymol. (Packer L. ed.) 251:8–28. Academic Press, San Diego, CA.
Fruton, J. S. and H. T. Clark. 1934. Chemical reactivity of cystine and its derivatives. J. Biol. Chem. 106:667–691.
Lowe, H. J. and W. M. Clark. 1956. Studies on oxidation-reduction. XXIV. Oxidation — reduction potentials of flavin adenine dinucleotide. J. Biol. Chem. 221:983–992.
Burton, K. and T. H. Wilson. 1953. The free-energy changes for the reduction of diphosphopyridine nucleotide and the dehydrogenation of L-malate and L-glycerol 1-phosphate. Biochem. J. 54:86.
Williams, M. H. and J. K. Yandell. 1982. Outer-sphere electron transfer reactions of ascorbate anions. Aust. J. Chem. 35:1133–1144.
De Vries, S., J. A. Berden and E, C. Slater, 1980. Properties of a semiquinone anion located in the QH2:cytochrome c oxidoreductase segment of the mitochondrial respiratory chain. FEBS Lett. 122:143–148.
Koppenol, W. H., J. J. Moreno, W. A. Pryor, H. Ischiropoulos and J. S. Beckman. 1992. Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide. Chem. Res. Toxicol. 5:834–842
Gilbert, H. F. 1990. Molecular and cellular aspects of thiol-disulfide exchange. In Advances in Enzymology, (Meister, A., ed.), pp. 69–173, Wiley Interscience, New York.
Matthews, J. R., N. Wakasugi, J. L. Virelizier, J. Yodoi and R. T. Hay. 1992. Thioredoxin regulates the DNA binding activity of NF-κB by reduction of a disulfide bond involving cysteine 62. Nucl. Acid Res. 20:821–3830.
Okamoto, T., H. Ogiwara, T. Hayashi, A. Mitsui, T. Kawabe and J. Yodoi. 1992. Human thioredoxin/adult T cell leukemia-derived factor activates the enhancer binding protein of human immunodeficiency virus type 1 by thiol redox control mechanism. Int. Immunol. 4:811–819.
Veech, R. L., L. V. Eggleston and H. A. Krebs. 1969. The redox state of free nicotinamide-adenine dinuleotide phosphate in the cytoplasm of rat liver. Biochem. J. 155:609–619.
Kirlin, W. G., J. Cai, S. A. Thompson, D. Diaz, T. J. Kavanagh and D. P. Jones. 1999. Glutathione redoxpotential in response to differentiation and enzyme inducers. Free Radic. Biol. Med. 27:1208–1218.
Follmann H. and I. Haeberlein. (1995/1996). Thioredoxin: universal, yet specific thiol-disulfide redox cofactors. BioFactors. 5:147–156.
Adler V., Y. Zhimin, K. D. Tew. and Z. Ronai Z. 1999. Role of redox potential and reactive oxygen species in stress signaling. Oncogene. 18:6104–6111.
Darzynkiewicz, Z., H. A. Crissman and J. P. Robinson eds. 1994. Methods in Cell Biology, 41 (Part A, Chap. 9), Flow Cytometry (2nd Edition). Academic Press, Inc, San Diego.
Musgrove, E. A. and D. W. Hedley. 1990. Measurement of intracellular pH. Methods in Cell Biology. 33:59–69.
Keyman, R. T. and E. J. Cragoe. 1988. Amiloride and its analogs as tools in the study of ion transport. J. Membrane Biol. 105:1–21.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2003 Kluwer Academic Publishers
About this chapter
Cite this chapter
Schafer, F.Q., Buettner, G.R. (2003). Redox State and Redox Environment in Biology. In: Forman, H.J., Fukuto, J., Torres, M. (eds) Signal Transduction by Reactive Oxygen and Nitrogen Species: Pathways and Chemical Principles. Springer, Dordrecht. https://doi.org/10.1007/0-306-48412-9_1
Download citation
DOI: https://doi.org/10.1007/0-306-48412-9_1
Publisher Name: Springer, Dordrecht
Print ISBN: 978-1-4020-1117-7
Online ISBN: 978-0-306-48412-4
eBook Packages: Springer Book Archive