NDLI: Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase.

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Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase.

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Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Pecht, I. Farver, O.
Description	Author Affiliation: Farver O ( Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.);
Abstract	Anaerobic reduction kinetics of the zucchini squash ascorbate oxidase (AO; L-ascorbate:oxygen oxidoreductase, EC 1.10.3.3) by pulse radiolytically produced CO2- radical ions were investigated. Changes in the absorption bands of type 1 [Cu(II)] (610 nm) and type 3 [Cu(II)] (330 nm) were monitored over a range of reactant concentrations, pH, and temperature. The direct bimolecular reduction of type 1 [Cu(II)] [(1.2 +/- 0.2) x 10(9) M-1.s-1] was followed by its subsequent reoxidation in three distinct phases, all found to be unimolecular processes with the respective specific rates of 201 +/- 8, 20 +/- 4, and 2.3 +/- 0.2 s-1 at pH 5.5 and 298 K. While at this pH no direct bimolecular reduction was resolved in the 330-nm band, at pH 7.0 such a direct process was observed [(6.5 +/- 1.2) x 10(8) M-1.s-1]. In the same slower time domains where type 1 [Cu(I)] reoxidation was monitored, reduction of type 3 [Cu(II)] was observed, which was also concentration independent and with identical rate constants and amplitudes commensurate with those of type 1 [Cu(II)] reoxidation. These results show that after electron uptake by type 1 [Cu(II)], its reoxidation takes place by intramolecular electron transfer to type 3 [Cu(II)]. The observed specific rates are similar to values reported for the limiting-rate constants of AO reduction by excess substrate, suggesting that internal electron transfer is the rate-determining step of AO activity. The temperature dependence of the intramolecular electron transfer rate constants was measured from 275 to 308 K at pH 5.5 and, from the Eyring plots, low activation enthalpies were calculated--namely, 9.1 +/- 1.1 and 6.8 +/- 1.0 kJ.mol-1 for the fastest and slowest phases, respectively. The activation entropies observed for these respective phases were -170 +/- 9 and -215 +/- 16 J.K-1.mol-1. The exceptionally low enthalpy barriers imply the involvement of highly optimized electron transfer pathways for internal electron transfer.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Ascorbate Oxidase Chemistry Amino Acid Sequence Copper Kinetics Molecular Sequence Data Molecular Structure Oxidation-Reduction Plants Enzymology Spectrum Analysis Thermodynamics Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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