Diverging Reaction Pathways and Key Intermediates in Ethylene Forming Enzyme DOI
Chao Wang, Elvira R. Sayfutyarova

The Journal of Physical Chemistry B, Journal Year: 2025, Volume and Issue: unknown

Published: April 24, 2025

Ethylene-forming enzyme (EFE) is a non-heme iron(II)- and 2-oxoglutarate-(Fe(II)/2OG)-dependent oxygenase with distinct catalytic reactivity. While most Fe(II)/2OG-dependent oxygenases catalyze substrate hydroxylation the 2OG decarboxylation to succinate, EFE primarily converts into CO2 ethylene. In this work, we employ multifaceted approach, including molecular dynamics, quantum mechanics methods, theoretical Mössbauer spectroscopy, analysis of intrinsic electric field exerted by protein environment, examine possible reaction pathways. Our study reveals novel second branch point, where ethylene formation (EF) 3-hydroxypropionate pathways diverge following Fe(III)-carbonate C3-C5-derived propion-3-yl radical intermediates, occurring earlier than suggested in previous studies. We identified multiple subsequent EF characterized low-energy barrier either Fe(II)-carbonates or Fe(II)-pyrocarbonates. Based on these findings, introduce revised mechanism for EFE, which consistent available experimental data highlights importance retaining C2-derived CO2, generated stages, within active site pathway. also intermediates that can produce quadrupole doublet peak observed recent experiments associated unidentified Fe(II)-containing species characteristic ethylene-forming This work provides new insights both first branchpoints pathway be useful modifications aimed at shifting product yield reaction.

Language: Английский

Diverging Reaction Pathways and Key Intermediates in Ethylene Forming Enzyme DOI
Chao Wang, Elvira R. Sayfutyarova

The Journal of Physical Chemistry B, Journal Year: 2025, Volume and Issue: unknown

Published: April 24, 2025

Ethylene-forming enzyme (EFE) is a non-heme iron(II)- and 2-oxoglutarate-(Fe(II)/2OG)-dependent oxygenase with distinct catalytic reactivity. While most Fe(II)/2OG-dependent oxygenases catalyze substrate hydroxylation the 2OG decarboxylation to succinate, EFE primarily converts into CO2 ethylene. In this work, we employ multifaceted approach, including molecular dynamics, quantum mechanics methods, theoretical Mössbauer spectroscopy, analysis of intrinsic electric field exerted by protein environment, examine possible reaction pathways. Our study reveals novel second branch point, where ethylene formation (EF) 3-hydroxypropionate pathways diverge following Fe(III)-carbonate C3-C5-derived propion-3-yl radical intermediates, occurring earlier than suggested in previous studies. We identified multiple subsequent EF characterized low-energy barrier either Fe(II)-carbonates or Fe(II)-pyrocarbonates. Based on these findings, introduce revised mechanism for EFE, which consistent available experimental data highlights importance retaining C2-derived CO2, generated stages, within active site pathway. also intermediates that can produce quadrupole doublet peak observed recent experiments associated unidentified Fe(II)-containing species characteristic ethylene-forming This work provides new insights both first branchpoints pathway be useful modifications aimed at shifting product yield reaction.

Language: Английский

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