Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate
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-oxoglutar...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Published: |
National Academy of Sciences
2017
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| _version_ | 1797102415017672704 |
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| author | Zhang, Z Smart, T Choi, H Hardy, F Lohans, C Abboud, M Richardson, M Paton, R McDonough, M Schofield, C |
| author_facet | Zhang, Z Smart, T Choi, H Hardy, F Lohans, C Abboud, M Richardson, M Paton, R McDonough, M Schofield, C |
| author_sort | Zhang, Z |
| collection | OXFORD |
| description | 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 non-oxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene rather than succinate formation. |
| first_indexed | 2024-03-07T06:05:42Z |
| format | Journal article |
| id | oxford-uuid:edc25e49-e4bb-4279-b265-dd8ac289f5bb |
| institution | University of Oxford |
| last_indexed | 2024-03-07T06:05:42Z |
| publishDate | 2017 |
| publisher | National Academy of Sciences |
| record_format | dspace |
| spelling | oxford-uuid:edc25e49-e4bb-4279-b265-dd8ac289f5bb2022-03-27T11:27:37ZStructural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarateJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:edc25e49-e4bb-4279-b265-dd8ac289f5bbSymplectic Elements at OxfordNational Academy of Sciences2017Zhang, ZSmart, TChoi, HHardy, FLohans, CAbboud, MRichardson, MPaton, RMcDonough, MSchofield, CEthylene 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 non-oxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene rather than succinate formation. |
| spellingShingle | Zhang, Z Smart, T Choi, H Hardy, F Lohans, C Abboud, M Richardson, M Paton, R McDonough, M Schofield, C Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate |
| title | Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate |
| title_full | Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate |
| title_fullStr | Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate |
| title_full_unstemmed | Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate |
| title_short | Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate |
| title_sort | structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2 oxoglutarate |
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