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Literature summary for 1.19.1.1 extracted from

  • Medina, M.; Gomez-Moreno, C.; Tollin, G.
    Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP+ reductase on the kinetics of interprotein electron transfer reactions (1992), Eur. J. Biochem., 210, 577-583.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Nostoc sp. P21890
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Nostoc sp. ATCC 29151 P21890
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer Nostoc sp. ?
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?
additional information no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer Nostoc sp. ATCC 29151 ?
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?
reduced flavodoxin + NADP+
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Nostoc sp. oxidized flavodoxin + NADPH + H+
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?
reduced flavodoxin + NADP+
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Nostoc sp. ATCC 29151 oxidized flavodoxin + NADPH + H+
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?

Cofactor

Cofactor Comment Organism Structure
FAD reduction of the FAD moiety of phenylglyoxal-modified FNR by laser-generated 5-deazariboflavin semiquinone occurs with a second-order rate constant 2.5fold smaller than that obtained for reduction of native FNR Nostoc sp.