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L-Arginine - OSTI GOV

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Last Updated: 05 February 2022

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An Iron(IV)–Oxo Intermediate Initiating l-Arginine Oxidation but Not Ethylene Production by the 2-Oxoglutarate-Dependent Oxygenase, Ethylene-Forming Enzyme

A four-electron oxidation conversion drastically different from the simpler decarboxylation of 2OG to succinate mediated by all other Fe/2OG enzymes in its major reaction. This large substrate deuterium kinetic isotope interaction has no effect on the EF:RO partition ratio; the pathways must diverge earlier. The Asp191Glu ligand substitution enzyme, which is consistent with this conclusion, accumulates four times as much of the ferryl complex as the wild-type enzyme and displays a 40-fold reduced EF:RO partition ratio, demonstrating a 40-fold decrease in the EF:RO partition ratio. One of four crystallographically defined L-Arg substrate/activator pairs that is unique to EFE among four crystallographically characterized L-Arg modifying Fe/2OG oxygenases, an active-site, like-charge guanidium pair, can help to selectively stabilize the transition state leading to the distinctive EF branch.

Source link: https://www.osti.gov/biblio/1774768

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions