Reduction of Substituted Flavins by ·CO⁻₂ and Cyclic Disulphide Anions

References

• Adams G.E., Wardman P. Free radical in biology: the pulse radiolysis approach. Free Radicals in Biology, W.A. Pryor. Academic Press, New York 1977; 3, chapter 2
   Google Scholar
• Ahmad R., Armstrong D.A. Reduction, oxidation, and addition reactions between free radicals and flavins. Biochemistry 1982; 21: 5445–5450
   PubMed Web of Science ®Google Scholar
• Ahmad R., Armstrong D.A. The effect of pH and complexation on redox reactions between RS radicals and flavins. Canadian Journal of Chemistry 1984; 62: 171–177
   Web of Science ®Google Scholar
• Akhlaq M.S., Sonntag V.C. Intermolecular H-abstraction of thiyl radicals from thiols and intramolecular complexing of the thiyl radical with the thiol group in 1,4-dithiothreitol. A pulse radiolysis study. Z. Naturforsch 1987; 42 C: 134–140
   Google Scholar
• Ashton W.T., Graham D.W., Brown R.D., Rogers E.F. Deaza isosteres of riboflavine and lumichrome. Tetrahedron Letters 1977; 30: 2551–2554
   Google Scholar
• Bliese M., Launikonis A., Loder J.W., Mau A.W.-H., Sasse W.H.F. Photoreduction of deazaflavin. Spectroscopic investigation. Australian Journal of Chemistry 1983; 36: 873–883
   Web of Science ®Google Scholar
• Breitenkamp M., Henglein A., Lilie J. Mechanism of the reduction of lead ions in aqueous solution (a pulse radiolysis study). Berichte der Bunsengesellschaft für Physikalische Chemie 1976; 80: 973–979
   Google Scholar
• Bruice T.C. Models and flavin catalysis. Progress in Bioorganic Chemistry 1976; 4: 2–87
   Google Scholar
• Buxton G.V., Sellers R.M. Acid dissociation constant of the carboxyl radical. Pulse radiolysis study of aqueous solutions of formic acid and sodium formate. Journal of the Chemical Society, Faraday Transactions I 1973; 69: 555–559
   Google Scholar
• Chan P.C., Bielski B.H.J. Pulse radiolysis study of optical absorption and kinetic properties of dithiothreitol free radical. Journal of the American Chemical Society 1973; 95: 5504–5508
   Web of Science ®Google Scholar
• Choong Y.S., Massey V. 2-Thioriboflavin 5′-phosphate (2-Thio-FMN) lactate oxidase. European Journal of Biochemistry 1983; 131: 501–508
   PubMedGoogle Scholar
• Claiborne A., Massey V., Fitzpatrick P.F., Schopfer L.M. 2-Thioflavins as active site probes of flavoproteins. Journal of Biological Chemistry 1982; 257: 174–182
   PubMed Web of Science ®Google Scholar
• Claiborne A., Hemmerich P., Massey V., Lawton R. Reaction of 2-Thio-FAD-reconstituted p-hydroxybenzoate hydroxylase with hydrogen peroxide. Journal of Biological Chemistry 1983; 258: 5433–5439
   PubMed Web of Science ®Google Scholar
• Clark W.M. Oxidation-reduction Potentials of Organic Systems. Williams and Wilkins, Baltimore 1960
   Google Scholar
• Draganić I.G., Draganić Z.D. The Radiation Chemistry of Water. Academic Press, New York 1971
   Google Scholar
• Duchstein H.-J., Fenner H., Hemmerich P., Knappe W.-R. (Photo)chemistry of 5-deazaflavin. A clue to the mechanism of flavin-dependent (De)hydrogenase. European Journal of Biochemistry 1979; 95: 167–181
   PubMedGoogle Scholar
• Elliot A.J., Wilkinson F., Armstrong D.A. A pulse radiolysis of zinc(II)-insulin. International Journal of Radiation Biology 1980; 38: 1–10
   Web of Science ®Google Scholar
• Gasgoine M., Radda G.K. The chemistry of flavins and flavoproteins. The reaction of dihydrolipoic acid with flavins. Biochimica et Biophysica Acta 1967; 131: 498–507
   PubMed Web of Science ®Google Scholar
• Goldberg M., Pecht I., Kramer H.E.A., Traber R., Hemmerich P. Structure and properties of 5-deazaflavin radicals as compared to natural flavosemiquinones. Biochimica et Biophysica Acta 1981; 673: 570–593
   PubMed Web of Science ®Google Scholar
• Hoffman M.Z., Hayon E. One-electron reduction of the disulfide linkage in aqueous solutions. Formation, protonation, and decay kinetics of RSSR- radical. Journal of the American Chemical Society 1972; 94: 7950–7957
   Web of Science ®Google Scholar
• Jayson G.G., Stirling D.A., Swallow A.J. Pulse- and X-radiolysis of 2-mercaptoethanol in aqueous solutions. International Journal of Radiation Biology 1971; 19: 143–156
   Web of Science ®Google Scholar
• Land E.J., Swallow A.J. One-electron reactions in biochemical systems as studied by pulse radiolysis. II. Riboflavin. Biochemistry 1969; 8: 2117–2125
   PubMed Web of Science ®Google Scholar
• Light D.R., Walsh C. Flavin analogs as mechanistic probes of adrenodoxin reductase-dependent electron transfer to the cholesterol side chain cleavage cytochrome P-450 of the adrenal cortex. Journal of Biological Chemistry 1980; 255: 4264–4277
   PubMed Web of Science ®Google Scholar
• Loechler E.L., Hollocher T.C. Mechanism of the reaction of dithiols with flavins. Journal of the American Chemical Society 1975; 97: 3235–3237
   PubMed Web of Science ®Google Scholar
• Müller F., Massey V., Hemmerich P., Lhoste J.-M., Gould D.C. The reduction of flavins by borohydride: 3,4-dihydroflavin. European Journal of Biochemistry 1969; 9: 392–401
   PubMedGoogle Scholar
• Redpath J.L. Pulse radiolysis of dithiothreitol. Radiation Research 1973; 51: 364–374
   Google Scholar
• Flavins and Flavoproteins, T.P. Singer. Elsevier, Amsterdam 1976
   Google Scholar
• Spencer R., Fisher J., Walsh C. One- and two-electron redox chemistry of 1-carba-1-deazariboflavin. Biochemistry 1977; 16: 3586–3594
   PubMed Web of Science ®Google Scholar
• Surdhar P.S., Armstrong D.A. Reactions of lumiflavin with amine radicals. Canadian Journal of Chemistry 1984; 63: 1357–1364
   Web of Science ®Google Scholar
• Surdhar P.S., Armstrong D.A. One-electron oxidation of dihydroflavin. Journal of Physical Chemistry 1985; 89: 5514–5518
   Web of Science ®Google Scholar
• Surdhar P.S., Armstrong D.A. Redox potentials of some sulfur-containing radicals. Journal of Physical Chemistry 1986; 90: 5915–5917
   Web of Science ®Google Scholar
• Surdhar P.S., Armstrong D.A., Massey V. The one- and two-electron reduction of 2-thioriboflavin by radical anions of CO2 and dithiothreitol. Canadian Journal of Chemistry 1986; 64: 76–70
   Web of Science ®Google Scholar
• Walsh C., Fisher J., Spencer R., Graham D.W., Ashton W.T., Brown J.E., Brown R.D., Rogers E.F. Chemical and enzymatic properties of riboflavin analogues. Biochemistry 1978; 17: 1942–1951
   PubMed Web of Science ®Google Scholar
• Williams C.H., Jr. Flavin-containing dehydrogenases. Enzymes 1976; 13: 89–173
   Google Scholar
• Wu Z., Ahmad R., Armstrong D.A. Formation of lipoamide anion radicals by hydroxyl, formate and alcohol radicals at pH 6–9. Radiation Physics and Chemistry 1984; 23: 251–257
   Web of Science ®Google Scholar