Hybrid radical-polar pathway for excision of ethylene from 2-oxoglutarate by an iron oxygenase
- Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.; OSTI
- Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
- Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Tracing a path to ethylene
Ethylene is produced industrially from fossil carbon sources, but plants and microbes produce small amounts through a handful of unusual enzymatic reactions. Copelandet al. studied a microbial ethylene-forming enzyme using oxygen isotope–tracing experiments and biochemical assays to test mechanistic proposals. This enzyme, which uses a non–heme iron center to activate oxygen, catalyzes two distinct oxidation reactions with different mechanisms. One reaction is entirely off-pathway and results in fragmentation of a co-substrate, arginine. The other reaction can completely fragment 2-oxoglutarate into ethylene, bicarbonate, and two molecules of carbon dioxide; however, it occasionally derails and yields an omega–hydroxy acid product. —MAF
- Research Organization:
- Pennsylvania State Univ., University Park, PA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC)
- DOE Contract Number:
- SC0016255;
- OSTI ID:
- 1852166
- Journal Information:
- Science, Journal Name: Science Journal Issue: 6562 Vol. 373; ISSN 0036-8075
- Publisher:
- AAAS
- Country of Publication:
- United States
- Language:
- English
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