Literature summary for 1.19.1.1 extracted from

Bonants, P.J.; M�ller, F.; Vervoort, J.; Edmondson, D.E.
A 31P�nuclear-magnetic�resonance study of NADPH-cytochrome-P-450 reductase and of the Azotobacter flavodoxin/ferredoxin-NADP+ reductase complex (1990), Eur. J. Biochem., 190, 531-537.

Crystallization (Commentary)

Crystallization (Comment)	Organism
no perturbation of the 31P-NMR resonances assigned to the FAD moiety of FNR or the FMN and phosphodiester moieties of Azotobacter flavodoxin are observed on complexation of Azotobacter flavodoxin and Spinacia oleracea FNR. Reduction of FMN to its semiquinone form results in extensive line-broadening of the FMN resonance. The FAD resonances of the FNR-flavodoxin complex are unaffected by FMN semiquinone formation. The distance from the FMN phosphate to the flavin ring is altered on binding the flavodoxin to FNR	Spinacia oleracea

Crystallization (Comment)

Organism

no perturbation of the 31P-NMR resonances assigned to the FAD moiety of FNR or the FMN and phosphodiester moieties of Azotobacter flavodoxin are observed on complexation of Azotobacter flavodoxin and Spinacia oleracea FNR. Reduction of FMN to its semiquinone form results in extensive line-broadening of the FMN resonance. The FAD resonances of the FNR-flavodoxin complex are unaffected by FMN semiquinone formation. The distance from the FMN phosphate to the flavin ring is altered on binding the flavodoxin to FNR

Spinacia oleracea

Organism

Organism	UniProt	Comment	Textmining
Spinacia oleracea	P00455	enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1	-

Synonyms

Synonyms	Comment	Organism
FNR	-	Spinacia oleracea

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Release 2023.1 (January 2023)