Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate

Greschner W, Lanzerath C, Reß T, Tenbrink K, Borchert S, Mix A, Hummel W, Gröger H (2014)
Journal of Molecular Catalysis B Enzymatic 103: 10-15.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
In this contribution the use of an artificial in situ-cofactor regeneration with [Fe(III)TSPPICI for enzymatic amino acid oxidation, exemplified for the L-glutamate dehydrogenase-catalyzed synthesis of a-ketoglutarate from sodium L-glutamate, is reported. In comparison of two L-glutamate dehydrogenases, the one isolated from Clostridium difficile turned out to be the preferred enzyme. At a substrate concentration of 15 mM of L-glutamate in situ-cofactor regeneration using [Fe(III)TSPP]CI as an "artificial NADH-oxidase" proceeded smoothly, leading to up to >99% overall conversion and 88% conversion related to the formation of alpha-ketoglutarate after 24h. At an increased concentration of 50 mM of L-glutamate, a somewhat decreased conversion of 43% was observed (which, however, corresponds to a nearly doubled volumetric productivity of 3.95 g/(Ld) compared to the experiments at 15 mM). Thus, the iron complex [Fe(III)TSPP]CI turned out to be capable to be used for cofactor regeneration of the cofactor NAD(+) for enzymatic amino acid oxidation. (C) 2014 Elsevier B.V. All rights reserved.
Stichworte
Amino acid dehydrogenase; Artificial cofactor recycling; Biomimetic; catalysis; Oxidation; alpha-Ketoglutarate
Erscheinungsjahr
2014
Zeitschriftentitel
Journal of Molecular Catalysis B Enzymatic
Band
103
Seite(n)
10-15
ISSN
1381-1177
Page URI
https://pub.uni-bielefeld.de/record/2681761

Zitieren

Greschner W, Lanzerath C, Reß T, et al. Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate. Journal of Molecular Catalysis B Enzymatic. 2014;103:10-15.
Greschner, W., Lanzerath, C., Reß, T., Tenbrink, K., Borchert, S., Mix, A., Hummel, W., et al. (2014). Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate. Journal of Molecular Catalysis B Enzymatic, 103, 10-15. doi:10.1016/j.molcatb.2013.12.015
Greschner, Wilko, Lanzerath, Carsten, Reß, Tina, Tenbrink, Katharina, Borchert, Sonja, Mix, Andreas, Hummel, Werner, and Gröger, Harald. 2014. “Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate”. Journal of Molecular Catalysis B Enzymatic 103: 10-15.
Greschner, W., Lanzerath, C., Reß, T., Tenbrink, K., Borchert, S., Mix, A., Hummel, W., and Gröger, H. (2014). Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate. Journal of Molecular Catalysis B Enzymatic 103, 10-15.
Greschner, W., et al., 2014. Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate. Journal of Molecular Catalysis B Enzymatic, 103, p 10-15.
W. Greschner, et al., “Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate”, Journal of Molecular Catalysis B Enzymatic, vol. 103, 2014, pp. 10-15.
Greschner, W., Lanzerath, C., Reß, T., Tenbrink, K., Borchert, S., Mix, A., Hummel, W., Gröger, H.: Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate. Journal of Molecular Catalysis B Enzymatic. 103, 10-15 (2014).
Greschner, Wilko, Lanzerath, Carsten, Reß, Tina, Tenbrink, Katharina, Borchert, Sonja, Mix, Andreas, Hummel, Werner, and Gröger, Harald. “Artificial cofactor regeneration with an iron(III)porphyrin as NADH-oxidase mimic in the enzymatic oxidation of L-glutamate to alpha-ketoglutarate”. Journal of Molecular Catalysis B Enzymatic 103 (2014): 10-15.
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