The ethylene-forming enzyme (EFE) is a bifunctional Fe(II)- and 2-(oxo)glutarate (Fe/2OG)-dependent enzyme. In its minor reaction (~30%), it activates O2 at its Fe(II) center to couple the decarboxylation of 2OG to CO2 and succinate to the hydroxylation of C5 of the substrate, L-arginine. In its major reaction (~70%), which requires L-arginine only as effector, EFE activates O2 to promote the fragmentation of 2OG to three equivalents for CO2/(bi)carbonate derived from C1, C2, and C5 and ethylene derived from the C3-C4 dimethylene unit [1].
We have studied this reaction by a combination of biochemical, analytical (LC/MS and GC/MS), rapid-kinetic and spectroscopic (stopped-flow absorption, stopped-flow FTIR, and freeze-quench Mössbauer), X-ray crystallographic, and computational methods [2-5]. Our studies provide detailed insight into the mechanisms of EFE. They also revealed a third reaction, viz the generation of 3-hydroxy-propionate (3HP) derived from the C3-C5 fragment of 2OG. Our studies are consistent with a mechanism, wherein the Fe(II)-persuccinate complex is the branchpoint of the arginine-oxidizing and ethylene-forming reactions. The ethylene-forming path proceeds via a succinylperoxycarbonato intermediate, which can undergo O-O homolysis, followed by β-scission of the ensuing succinyl radical to generate a propionate-3-yl radical. Our results suggest that the latter intermediate is the second branchpoint, which can either undergo C4-C5 scission to yield ethylene or it can couple to the C1-derived (bi)carbonato ligand to generate a carbonate-monoester, which eliminates the alternative 3HP product.
Financial support by the Department of Energy (DOE BES-DE-SC0016255) is gratefully acknowledged.
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