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Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate.


ABSTRACT: Ethylene is important in industry and biological signaling. In plants, ethylene is produced by oxidation of 1-aminocyclopropane-1-carboxylic acid, as catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase. Bacteria catalyze ethylene production, but via the four-electron oxidation of 2-oxoglutarate to give ethylene in an arginine-dependent reaction. Crystallographic and biochemical studies on the Pseudomonas syringae ethylene-forming enzyme reveal a branched mechanism. In one branch, an apparently typical 2-oxoglutarate oxygenase reaction to give succinate, carbon dioxide, and sometimes pyrroline-5-carboxylate occurs. Alternatively, Grob-type oxidative fragmentation of a 2-oxoglutarate-derived intermediate occurs to give ethylene and carbon dioxide. Crystallographic and quantum chemical studies reveal that fragmentation to give ethylene is promoted by binding of l-arginine in a nonoxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene, relative to succinate formation.

SUBMITTER: Zhang Z 

PROVIDER: S-EPMC5422762 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate.

Zhang Zhihong Z   Smart Tristan J TJ   Choi Hwanho H   Hardy Florence F   Lohans Christopher T CT   Abboud Martine I MI   Richardson Melodie S W MSW   Paton Robert S RS   McDonough Michael A MA   Schofield Christopher J CJ  

Proceedings of the National Academy of Sciences of the United States of America 20170418 18


Ethylene is important in industry and biological signaling. In plants, ethylene is produced by oxidation of 1-aminocyclopropane-1-carboxylic acid, as catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase. Bacteria catalyze ethylene production, but via the four-electron oxidation of 2-oxoglutarate to give ethylene in an arginine-dependent reaction. Crystallographic and biochemical studies on the <i>Pseudomonas syringae</i> ethylene-forming enzyme reveal a branched mechanism. In one branch, a  ...[more]

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