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. 2013 Oct 4;3(10):10.1021/cs400087p.
doi: 10.1021/cs400087p.

Mechanism and Catalytic Diversity of Rieske Non-Heme Iron-Dependent Oxygenases

Sarah M Barry  1 , Gregory L Challis
Affiliations

Mechanism and Catalytic Diversity of Rieske Non-Heme Iron-Dependent Oxygenases

Sarah M Barry et al. ACS Catal. .

Abstract

Rieske non-heme iron-dependent oxygenases are important enzymes that catalyze a wide variety of reactions in the biodegradation of xenobiotics and the biosynthesis of bioactive natural products. In this perspective article, we summarize recent efforts to elucidate the catalytic mechanisms of Rieske oxygenases and highlight the diverse range of reactions now known to be catalyzed by such enzymes.

Keywords: Amine Oxidation; Biodegradation; Biosynthesis; C-H functionalization; Dihydroxylation; Oxidative Cyclisation.

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Figures

Figure 1
Figure 1
Reaction catalyzed by naphthalene dioxygenase (top) and architecture of the [2Fe-2S] (green) and non-heme iron (purple) centers within the α-subunits of the enzyme suggested by X-ray crystallographic analysis. A conserved aspartate residue (red) serves as a bridge between the (presumably reduced) [2Fe-2S] center and the non-heme iron center in adjacent α-subunits within the α3β3 enzyme complex.
Figure 2
Figure 2
Proposed catalytic mechanisms for naphthalene dioxygenase. The question of whether the Fe(III)-OOH complex reacts directly with the substrate or whether it undergoes rearrangement to an Fe(V)=O(OH) complex first remains unresolved.
Figure 3
Figure 3
Structure of a synthetic complex designed to mimic the [2Fe-2S] cluster in Rieske oxygenases.
Figure 4
Figure 4
Structures of the TMC ligand and the TMC-Fe(III)-hydroperoxide complex.
Figure 5
Figure 5
Structures of TAML-Fe(V)=O, the first non heme Fe(V)=O complex to be characterized, and the BQEN ligand.
Figure 6
Figure 6
First example of alkene cis-dihydroxylation by a Fe(V)=O(OH) model complex.
Figure 7
Figure 7
Hydroxylation reactions catalyzed by KshAB in M. tuberculosis cholesterol catabolism. AD: 4-androstene-3, 17-dione; ADD: 1,4-androstadiene-3,17-dione.
Figure 8
Figure 8
Desaturation of cholesterol catalyzed by DAF-36 in vitro. The essential role for survival of nematodes and insects played by DAF-36 in vivo is unclear.
Figure 9
Figure 9
O-Demethylation reaction catalyzed by dicamba O-demethylase, the first step in the degradation of the herbicide dicamba in plants.
Figure 10
Figure 10
Degradation of caffeine catalyzed by NdmA and NdmB to form 7-methylxanthine. Electrons are supplied to NdmA and NdmB by the NADH-dependent reductase NdmB.
Figure 11
Figure 11
Reaction catalyzed by PrnD in pyrrolnitrin biosynthesis.
Figure 12
Figure 12
Incorporation of labeled dioxygen into intermediates and/or the product during PrnD-catalysed oxidation of 4-aminobenzylamine (A) and 4-hydroxylaminobenzylamine (B).
Figure 13
Figure 13
Regio- and stereodivergent oxidative carbocyclization reactions catalyzed by the Rieske oxygenase-like enzymes RedG and McpG in streptroubin B and metacycloprodigiosin biosynthesis, respectively.
Figure 14
Figure 14
Proposed catalytic mechanisms for the RedG-catalyzed oxidative carbocyclization of undecylprodigiosin to form streptorubin B. As for naphthalene dioxygenase, it is unclear whether the Fe(III)-OOH complex reacts directly with the substrate or undergoes rearrangement to an Fe(V)=O(OH) complex prior to reacting.
Figure 15
Figure 15
Large-scale cis-dihydroxylation of methyl cinnamate catalyzed by FeIII(N4Me2)Cl2. Epoxide and α-hydroxyketone byproducts are also formed in small amounts.
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