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Título

Comparison of the Kinetics of Reduction and Intramolecular Electron Transfer in Electrostatic and Covalent Complexes of Ferredoxin-NADP+ Reductase and Flavodoxin from Anabaena PCC 7119

AutorWalker, Mark C.; Pueyo, José Javier ; Gómez-Moreno, Carlos
Palabras claveIntramolecular Electron Transfer
Electro Transfer in Electrostatic
Covalent Complexes
Ferredoxin-NADP+
Reductase and Flavodoxin
Anabaena PCC 7119
Fecha de publicación1990
EditorAcademic Press
CitaciónArchives of Biochemistry and Biophysics 281 (1): 76-83 (1990)
ResumenThe kinetics of reduction and intracomplex electron transfer in electrostatically stabilized and covalently crosslinked complexes between ferredoxin-NADP+ reductase (FNR) and flavodoxin (Fld) from the cyanobacterium Anabuena PCC 7119 were compared using laser flash photolysis. The second-order rate constant for reduction by 5-deazariboflavin semiquinone (dRfII) of FNR within the electrostatically stabilized complex at 10 mM ionic strength (4.0 X 10s M-’ s-‘) was identical to that for free FNR. This suggests that the FAD cofactor of FNR is not sterically hindered upon complex formation. A lower limit of approximately 7000 s-l was estimated for the first-order rate constant for intracomplex electron transfer from FNRmd to Fl&, under these conditions. In contrast, for the covalently crosslinked complex, a smaller secondorder rate constant (2.1 X lo* M-’ s-l) was obtained for the reduction of FNR by dRfII within the complex, suggesting that some steric hindrance of the FAD cofactor of FNR occurs due to crosslinking. A limiting rate constant of 1000 s-l for the intracomplex electron transfer reaction was obtained for the covalent complex, which was unaffected by changes in ionic strength. The substantially diminished limiting rate constant, relative to that of the electrostatic complex, may reflect either a suboptimal orientation of the redox cofactors within the covalent complex or a required structural reorganization preceding electron transfer which is not allowed once the proteins have been covalently linked. Thus, although the covalent complex is biochemically competent, it is not a quantitatively precise model for the catalytically relevant intermediate along the reaction pathway.
Descripción8 pages, figures, and tables statistics.
URIhttp://hdl.handle.net/10261/26062
ISSN0003-9861
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