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Published on: March 18, 2012

Substrate activation by iron superoxo intermediates.

Wilfred A van der Donk¹, Carsten Krebs, J Martin Bollinger

¹Department of Chemistry and Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, 600 S. Mathews Ave, Urbana, IL 61801, USA. vddonk@uiuc.edu

Current Opinion in Structural Biology

|October 19, 2010

Summary

This summary is machine-generated.

Non-heme iron enzymes use a novel Fe(III)-superoxide mechanism for oxidation, bypassing the traditional Fe(IV)-oxo intermediate. This pathway enables complex reactions without consuming reducing agents, revealing unifying principles in enzyme catalysis.

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Published on: February 24, 2018

Area of Science:

Biochemistry
Bioinorganic Chemistry
Enzymology

Background:

Traditional mechanistic paradigms for non-heme iron oxygenases and oxidases involve a single C-H-bond-cleaving intermediate of the Fe(IV)-oxo (ferryl) type.
This paradigm is insufficient to explain the observed chemistry in a growing number of enzymatic reactions.

Purpose of the Study:

To explore and discuss examples of a novel mechanistic strategy employed by non-heme iron enzymes.
To identify unifying principles underlying these alternative oxidation pathways.

Main Methods:

Review and analysis of experimental data from various non-heme iron oxygenase and oxidase systems.
Comparison of proposed mechanisms with established paradigms.

Main Results:

Fe(III)-superoxide complexes, formed by O(2) addition to the Fe(II) cofactor, initiate substrate oxidation via hydrogen abstraction in several enzyme systems.
This alternative route allows for complex oxidation reactions without the need for external reducing equivalents.

Conclusions:

The Fe(III)-superoxide pathway represents a significant alternative to the Fe(IV)-oxo intermediate in non-heme iron enzyme catalysis.
Understanding this novel mechanism provides new insights into the versatility and efficiency of enzymatic oxidation reactions.