Photobiocatalytic decarboxylation for olefin synthesis

Zachos, Ioannis; Gaßmeyer, Sarah Katharina; Bauer, Daniel P.; Sieber, Volker; Hollmann, Frank; Kourist, Robert

doi:10.1039/c4cc07276f

Cited by 103 publications

(111 citation statements)

References 31 publications

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“…Whereas self-sufficient P450s show the highest turnover numbers and coupling efficiency up to now, fusion to redox partners or modern electron donor systems allow also other CYPs to run with increased efficiency [94,125,131,132]. Drawbacks of the CYP family are poor (regio-)selectivities, low productivities, uncoupling, and the dependence on NADPH as reducing agent [14,17,18].…”

Section: Discussionmentioning

confidence: 99%

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

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Section: Discussionmentioning

confidence: 99%

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

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“…OleT JE was reported to catalyse 97% conversion of 200 µM myristic acid (C14:0) in the presence of 500 µM H 2 O 2 (7). However, on an industrial scale excess H 2 O 2 may inhibit enzymatic activity (13). This phenomenon was demonstrated…”

Section: Introductionmentioning

confidence: 97%

Production of alkenes and novel secondary products by P450 OleT_JE using novel H₂O₂‐generating fusion protein systems

et al. 2017

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Jeotgalicoccus sp. 8456 OleT JE (CYP152L1) is a fatty acid decarboxylase cytochrome P450 that uses hydrogen peroxide (H 2 O 2 ) to catalyse production of terminal alkenes, which are industrially important chemicals with biofuel applications. We report enzyme fusion systems in which Streptomyces coelicolor alditol oxidase (AldO) is linked to OleT JE . AldO oxidizes polyols (including glycerol), generating H 2 O 2 as a co-product and facilitating its use for efficient OleT JE -dependent fatty acid decarboxylation. AldO activity is regulatable by polyol substrate titration, enabling control over H 2 O 2 supply to minimise oxidative inactivation of OleT JE and prolong activity for increased alkene production. We also use these fusion systems to generate novel products from secondary turnover of 2-OH and 3-OH myristic acid primary products, expanding the catalytic repertoire of OleT JE .

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“…The predisposition of OleT to generate a substantial proportion of fatty alcohol products with shorter, nonphysiological substrates (36,38) highlights that the enzyme is able to simultaneously function as an oxygenase. We propose, based on analogy to mechanisms purported for desaturases, which can also exhibit dual functionality (reviewed in ref.…”

Section: Significancementioning

confidence: 99%

“…1). In addition to the peculiar chemical nature of this reaction, OleT catalysis has garnered significant biotechnological interest, as it involves the conversion of a bioavailable and abundant feedstock into a petrochemical and valuable synthetic precursor (36)(37)(38). OleT differs from most P450s in two fundamental aspects.…”

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“…Belonging to the CYP152 family (39, 40), catalysis is efficiently initiated by hydrogen peroxide, rather than O 2 and reducing equivalents delivered through a redox chain. Moreover, single (35) and multiple turnover (36,38) studies of what is generally believed to approximate the chain length of the physiological substrate, eicosanoic acid (EA), have indicated that oxidative decarboxylation, affording nonadecene, is the largely dominant reaction route (34). Combined 13 C substrate and H 2 18 O 2 isotopic labeling by our laboratory has shown that cleavage of the terminal fatty acid carboxylate does not lead to recovery of 18 O in…”

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Catalytic strategy for carbon−carbon bond scission by the cytochrome P450 OleT

Grant

Mitchell

Makris

2016

Proc. Natl. Acad. Sci. U.S.A.

102

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OleT is a cytochrome P450 that catalyzes the hydrogen peroxidedependent metabolism of C n chain-length fatty acids to synthesize C n-1 1-alkenes. The decarboxylation reaction provides a route for the production of drop-in hydrocarbon fuels from a renewable and abundant natural resource. This transformation is highly unusual for a P450, which typically uses an Fe 4+ −oxo intermediate known as compound I for the insertion of oxygen into organic substrates. OleT, previously shown to form compound I, catalyzes a different reaction. A large substrate kinetic isotope effect (≥8) for OleT compound I decay confirms that, like monooxygenation, alkene formation is initiated by substrate C−H bond abstraction. Rather than finalizing the reaction through rapid oxygen rebound, alkene synthesis proceeds through the formation of a reaction cycle intermediate with kinetics, optical properties, and reactivity indicative of an Fe 4+ −OH species, compound II. The direct observation of this intermediate, normally fleeting in hydroxylases, provides a rationale for the carbon−carbon scission reaction catalyzed by OleT.C ytochrome P450 (CYP) enzymes catalyze an extraordinary breadth of physiologically important oxidations for xenobiotic detoxification and specialized biosynthetic pathways (1, 2). The metabolic diversity of CYP enzymes originates from a sophisticated interplay of substrate molecular recognition with precise tuning of metal oxygen species formed at the enzyme active site. CYPs use a thiolate-ligated heme iron cofactor to activate molecular oxygen and produce short-lived ferric superoxo (3-5), ferric (hydro)peroxo (6-8), and ferryl (9, 10) intermediates. Coordinated efforts over several decades have resulted in isolation of each intermediate, including recent characterization of the principal oxidant thought to be responsible for the vast majority of P450 oxidations, the Fe 4+ −oxo pi−cation radical species commonly referred to as compound I (or P450-I) (10).The archetypal P450 hydroxylation involves C−H bond abstraction by P450-I and ensuing rapid oxygen insertion through a recombination process termed "oxygen rebound" (11, 12). The hydrogen abstraction/rebound mechanism describes the strategy used for most P450 transformations, and is thought to describe catalysis by numerous metal-dependent oxygenases and synthetic bio-inspired metal−oxo complexes (e.g., refs. 13-17). Despite the ubiquity of this mechanism, in some metalloenzymes, a metal−oxo species is formed that is not ultimately destined for incorporation into a substrate. Some characterized examples include the nonheme dinuclear iron ribonucleotide reductase (RNR R2) (18,19) and mononuclear iron halogenase SyrB2 (20-22). The mechanisms for RNR and SyrB2 highlight the importance of quaternary structural elements, an extensive 35-Å proton-coupled electron transfer pathway in RNR (23), and extremely subtle (subangstrom) substrate positional tuning (SyrB2) (21,22), to enable efficient circumvention from the monooxygenation reaction coordinate.P450-I has also been link...

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Photobiocatalytic decarboxylation for olefin synthesis

Cited by 103 publications

References 31 publications

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Production of alkenes and novel secondary products by P450 OleT_JE using novel H₂O₂‐generating fusion protein systems

Catalytic strategy for carbon−carbon bond scission by the cytochrome P450 OleT

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Photobiocatalytic decarboxylation for olefin synthesis

Cited by 103 publications

References 31 publications

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2‐generating fusion protein systems

Catalytic strategy for carbon−carbon bond scission by the cytochrome P450 OleT

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Production of alkenes and novel secondary products by P450 OleT_JE using novel H₂O₂‐generating fusion protein systems