Towards [Cp∗Rh(bpy)(H2O)]2+-promoted P450 catalysis: Direct regeneration of CytC

Hollmann, Frank; Schmid, Andreas

doi:10.1016/j.jinorgbio.2008.11.005

Cited by 27 publications

(23 citation statements)

References 23 publications

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“…A broad set of cofactor regeneration methods has been successfully developed in the last years. Besides enzymatic cofactor regenerations, electrochemical substituting (Çekiç et al, ; Ley et al, ; Reipa et al, ; Udit et al, ) and chemocatalytic cofactor regenerations (Hollmann and Schmid, ; Kölle and Grützel, ; Ruppert et al, ) have also been reported. In this study the surface displayed P450BM3 were combined with electrochemical, chemical and enzymatic regeneration systems.…”

Section: Resultsmentioning

confidence: 99%

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

Ströhle

Kranen²,

Schrader

et al. 2015

Biotech & Bioengineering

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New production routes for fine and bulk chemicals are important to establish further sustainable processes in industry. Besides the identification of new biocatalysts and new production routes the optimization of existing processes in regard to an improved utilization of the catalysts are needed. In this paper we describe the successful expression of P450BM3 on the surface of E. coli cells with the Autodisplay system. The successful hydroxylation of palmitic acid by using surface-displayed P450BM3 was shown. Besides optimization of surface protein expression, several cofactor regeneration systems were compared and evaluated. Afterwards, the development of a suitable process for the biocatalytic hydroxylation of fatty acids based on the re-use of the catalysts after a simple centrifugation was investigated. It was shown that the catalyst can be used for several times without any loss in activity. By using surface-displayed P450s in combination with an enzymatic cofactor regeneration system a total turnover number of up to 54,700 could be reached, to the knowledge of the authors the highest value reported for a P450 monooxygenase to date. Further optimizations of the described reaction system can have an enormous impact on the process design for more sustainable bioprocesses. Biotechnol. Bioeng. 2016;113: 1225-1233. © 2015 Wiley Periodicals, Inc.

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Section: Resultsmentioning

confidence: 99%

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

Ströhle

Kranen²,

Schrader

et al. 2015

Biotech & Bioengineering

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“…A more elegant approach is to deliver the reducing equivalents directly from the cosubstrate to the oxidoreductases, thereby shortcutting the complicated natural electron transport chain. Ever since the pioneering work by Vilker and coworkers 14 , a range of direct regeneration approaches have been reported [15][16][17][18][19][20][21][22][23][24][25][26][27][28] .…”

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confidence: 99%

Photobiocatalytic chemistry of oxidoreductases using water as the electron donor

et al. 2014

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To date, water has been poorly studied as the sacrificial electron donor for biocatalytic redox reactions using isolated enzymes. Here we demonstrate that water can also be turned into a sacrificial electron donor to promote biocatalytic redox reactions. The thermodynamic driving force required for water oxidation is obtained from UV and visible light by means of simple titanium dioxide-based photocatalysts. The electrons liberated in this process are delivered to an oxidoreductase by simple flavin redox mediators. Overall, the feasibility of photobiocatalytic, water-driven bioredox reactions is demonstrated.

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“…Formate would be a more suitable reductant for the reductive activation of O 2 (generating only 44 g of volatile and therefore not accumulating CO 2 waste per mol H 2 O 2 equivalent). The systems available today, however, either rely on bioincompatible transition‐metal catalysts, or are too complex or too elaborate to be practical.…”

Section: Methodsmentioning

confidence: 99%

Formate Oxidase (FOx) from Aspergillus oryzae: One Catalyst Enables Diverse H₂O₂‐Dependent Biocatalytic Oxidation Reactions

et al. 2019

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An increasing number of biocatalytic oxidation reactions rely on H 2 O 2 as a clean oxidant. The poor robustness of most enzymes towards H 2 O 2 , however, necessitates more efficient systems for in situ H 2 O 2 generation. In analogy to the well‐known formate dehydrogenase to promote NADH‐dependent reactions, we here propose employing formate oxidase (FOx) to promote H 2 O 2 ‐dependent enzymatic oxidation reactions. Even under non‐optimised conditions, high turnover numbers for coupled FOx/peroxygenase catalysis were achieved.

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Towards [Cp∗Rh(bpy)(H2O)]2+-promoted P450 catalysis: Direct regeneration of CytC

Cited by 27 publications

References 23 publications

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

Photobiocatalytic chemistry of oxidoreductases using water as the electron donor

Formate Oxidase (FOx) from Aspergillus oryzae: One Catalyst Enables Diverse H₂O₂‐Dependent Biocatalytic Oxidation Reactions

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Towards [Cp∗Rh(bpy)(H2O)]2+-promoted P450 catalysis: Direct regeneration of CytC

Cited by 27 publications

References 23 publications

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

Photobiocatalytic chemistry of oxidoreductases using water as the electron donor

Formate Oxidase (FOx) from Aspergillus oryzae: One Catalyst Enables Diverse H2O2‐Dependent Biocatalytic Oxidation Reactions

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Formate Oxidase (FOx) from Aspergillus oryzae: One Catalyst Enables Diverse H₂O₂‐Dependent Biocatalytic Oxidation Reactions