Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase

Maid, Harald; Boehm, Philipp; Huber, Stefan M.; Bauer, Walter; Hummel, Werner; Jux, Norbert; Gröger, Harald

Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase

Maid H, Boehm P, Huber SM, Bauer W, Hummel W, Jux N, Gröger H (2011)
Angewandte Chemie International Edition 50(10): 2397-2400.

Zeitschriftenaufsatz | Veröffentlicht | Englisch

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DOI

https://doi.org/10.1002/anie.201004101

Autor*in

Maid, Harald; Boehm, Philipp; Huber, Stefan M.; Bauer, Walter; Hummel, Werner^UniBi; Jux, Norbert; Gröger, Harald^UniBi

Einrichtung

Fakultät für Chemie > Industrielle Organische Chemie und Biotechnologie

Erscheinungsjahr

2011

Zeitschriftentitel

Angewandte Chemie International Edition

Band

50

Ausgabe

10

Seite(n)

2397-2400

ISSN

1433-7851

Page URI

https://pub.uni-bielefeld.de/record/2344721

Zitieren

Maid H, Boehm P, Huber SM, et al. Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase. Angewandte Chemie International Edition. 2011;50(10):2397-2400.

Maid, H., Boehm, P., Huber, S. M., Bauer, W., Hummel, W., Jux, N., & Gröger, H. (2011). Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase. Angewandte Chemie International Edition, 50(10), 2397-2400. https://doi.org/10.1002/anie.201004101

Maid, Harald, Boehm, Philipp, Huber, Stefan M., Bauer, Walter, Hummel, Werner, Jux, Norbert, and Gröger, Harald. 2011. “Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase”. Angewandte Chemie International Edition 50 (10): 2397-2400.

Maid, H., Boehm, P., Huber, S. M., Bauer, W., Hummel, W., Jux, N., and Gröger, H. (2011). Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase. Angewandte Chemie International Edition 50, 2397-2400.

Maid, H., et al., 2011. Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase. Angewandte Chemie International Edition, 50(10), p 2397-2400.

H. Maid, et al., “Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase”, Angewandte Chemie International Edition, vol. 50, 2011, pp. 2397-2400.

Maid, H., Boehm, P., Huber, S.M., Bauer, W., Hummel, W., Jux, N., Gröger, H.: Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase. Angewandte Chemie International Edition. 50, 2397-2400 (2011).

Maid, Harald, Boehm, Philipp, Huber, Stefan M., Bauer, Walter, Hummel, Werner, Jux, Norbert, and Gröger, Harald. “Iron Catalysis for In Situ Regeneration of Oxidized Cofactors by Activation and Reduction of Molecular Oxygen: A Synthetic Metalloporphyrin as a Biomimetic NAD(P)H Oxidase”. Angewandte Chemie International Edition 50.10 (2011): 2397-2400.

Daten bereitgestellt von European Bioinformatics Institute (EBI)

11 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Asymmetric Chemoenzymatic Reductive Acylation of Ketones by a Combined Iron-Catalyzed Hydrogenation-Racemization and Enzymatic Resolution Cascade.
El-Sepelgy O, Brzozowska A, Rueping M., ChemSusChem 10(8), 2017
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Dehydrogenase-Catalyzed Oxidation of Furanics: Exploitation of Hemoglobin Catalytic Promiscuity.
Jia HY, Zong MH, Yu HL, Li N., ChemSusChem 10(18), 2017
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Characterization of Biomimetic Cofactors According to Stability, Redox Potentials, and Enzymatic Conversion by NADH Oxidase from Lactobacillus pentosus.
Nowak C, Pick A, Csepei LI, Sieber V., Chembiochem 18(19), 2017
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Enzyme Mimics: Advances and Applications.
Kuah E, Toh S, Yee J, Ma Q, Gao Z., Chemistry 22(25), 2016
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New artificial fluoro-cofactor of hydride transfer with novel fluorescence assay for redox biocatalysis.
Zhang L, Yuan J, Xu Y, Zhang YH, Qian X., Chem Commun (Camb) 52(38), 2016
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Merging Iron Catalysis and Biocatalysis-Iron Carbonyl Complexes as Efficient Hydrogen Autotransfer Catalysts in Dynamic Kinetic Resolutions.
El-Sepelgy O, Alandini N, Rueping M., Angew Chem Int Ed Engl 55(43), 2016
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Soldevila-Barreda JJ, Sadler PJ., Curr Opin Chem Biol 25(), 2015
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A water-forming NADH oxidase from Lactobacillus pentosus suitable for the regeneration of synthetic biomimetic cofactors.
Nowak C, Beer B, Pick A, Roth T, Lommes P, Sieber V., Front Microbiol 6(), 2015
PMID: 26441891

Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes.
Köhler V, Wilson YM, Dürrenberger M, Ghislieri D, Churakova E, Quinto T, Knörr L, Häussinger D, Hollmann F, Turner NJ, Ward TR., Nat Chem 5(2), 2013
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Iron-catalyzed hydrogenation for the in situ regeneration of an NAD(P)H model: biomimetic reduction of α-keto-/α-iminoesters.
Lu LQ, Li Y, Junge K, Beller M., Angew Chem Int Ed Engl 52(32), 2013
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