The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Fluorescence and optical characteristics of reduced flavines and flavoproteins
Open accessAbstract
The fluorescence and absorption properties of a series of reduced flavoproteins have been measured and compared with the properties of suitable model compounds. Contrary to common belief, a number of reduced flavoproteins have been found to exhibit appreciable fluorescence emission with maxima in the range 500-530 nm. In keeping with common observation, the reduced model flavines are devoid of fluorescence in solution at room temperature, but show marked fluorescence emission in the range 476-512 nm at 77°K in rigid glasses. The fluorescence quantum yield of reduced lactate oxidase (emission λmax 507 nm) is increased 4.7 times upon formation of covalent N5 adducts and the emission maximum is shifted to 476 nm. In the case of the nonfluorescent reduced D-amino acid oxidase, formation of covalent adducts leads to appearance of a fluorescence emission maximal at 520 nm. Among the enzymes investigated the absorption spectra of the reduced forms vary markedly. The chromophore of the reduced flavine was found to be very sensitive to variations of the polarity, pH, or viscosity of the solvent and to substitution. An attempt is made to interpret the absorption and fluorescence emission spectra and to correlate the mentioned effects. Thus valid information about the protein environment at the flavine binding site may be obtained. In particular, in the case of fluorescent-reduced enzymes, the vibrational mobility of the reduced flavocoenzyme is restricted by the protein.
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Cites
Purification and Properties of the Glucose Oxidase from Aspergillus niger
Swoboda, B. E. P., & Massey, V. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97448-x · Cited by 515
Self-citationOn the Reaction Mechanism of Yeast Glutathione Reductase
Massey, V., & Williams, C. H. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97085-7 · Cited by 488
Self-citationMassey, V., & Palmer, G. (1966) · Biochemistry · doi:10.1021/bi00874a016 · Cited by 452
Self-citationFluorescence of riboflavin and flavin-adenine dinucleotide
Weber, G. (1950) · Biochemical Journal · doi:10.1042/bj0470114 · Cited by 402
The Reactivity of Flavoproteins with Sulfite
Massey, V, Müller, F., Feldberg, R., Schuman, M., Sullivan, P. A., Howell, L. G., Mayhew, S. G., Matthews, R. G., & Foust, G. P. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36376-7 · Cited by 343
Self-citationLambeth, D. O., & Palmer, G. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43514-x · Cited by 317
Molecular luminescence studies of flavines. I. Excited states of flavines
Sun, M., Moore, T. A., & Song, P.-S. (1972) · Journal of the American Chemical Society · doi:10.1021/ja00760a052 · Cited by 254
Light-mediated reduction of flavoproteins with flavins as catalysts
Massey, V., Stankovich, M. T., & Hemmerich, P. H. (1978) · Biochemistry · doi:10.1021/bi00594a001 · Cited by 175
Self-citationCatalysis of Oxidation of Nitrogen Compounds by Flavin Coenzymes in the Presence of Light
Frisell, W. R., Chung, C. W., & Mackenzie, C. G. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98176-7 · Cited by 160
Oxidation-Reduction Properties of Flavodoxin from Peptostreptococcus elsdenii
Mayhew, S. G., Foust, G. P., & Massey, V. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91859-4 · Cited by 130
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Metadata
- Authors
- Ghisla, S., Massey, V., Lhoste, J.-M., & Mayhew, S. G.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1974-01-01
- Volume
- 13
- Issue
- 3
- Pages
- 589-597
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1996811682
- Cited by
- 386
- References
- 17
- FWCI
- 10.23
- Type
- journal article
- Language
- en
- Open access
- green
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