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Catalysts
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Biomimetic Catalysts
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Biomimetic Catalysts

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: closed (15 January 2013) | Viewed by 33510

Special Issue Editor

Prof. Dr. Armando Córdova

E-Mail Website
Guest Editor
1. Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, 106 91 Stockholm, Sweden
2. Department of Natural Sciences, Engineering and Mathematics, Mid Sweden University, 851 70 Sundsvall, Sweden
Interests: asymmetric catalysis; biomimetic catalysis; organocatalysis; biocatalysis; vombination of organo- and transition metal catalysis; domino, tandem cascade reactions; development of environmentally friendly catalytic reactions; catalytic modification of cellulose and polysaccharides; asymmetric synthesis; diversity oriented synthesis

Special Issue Information

Dear Colleagues,

Nature has always been a great inspiration for synthetic chemists in finding new ways of preparing their molecules and reactions. Catalysis is arguably one of the most efficient, economic and environmentally benign ways of assemble useful molecules and materials for the betterment of human health. In fact, it is the foundation for the perfectly evolved biochemical pathways of the cell and consequently life. Thus, lessons from how natural catalysts operate can therefore be very important for the design of the next generation of catalysts and chemical processes. In this special issue, some of the state of the art in the broad field of “biomimetic catalysis” is presented.

Prof. Dr. Armando Córdova
Guest Editor

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Keywords

  • biomimetic catalysis/catalyze
  • mimic biological system
  • biosynthesis
  • metalloporphyrin (Porphyrin)
  • cytochrome P-450

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Published Papers (4 papers)

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Research

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316 KiB  
Article
Biomimetic Catalysts for Oxidation of Veratryl Alcohol, a Lignin Model Compound
by Gustavo González-Riopedre, María Isabel Fernández-García, Esther Gómez-Fórneas and Marcelino Maneiro
Catalysts 2013, 3(1), 232-246; https://doi.org/10.3390/catal3010232 - 4 Mar 2013
Cited by 21 | Viewed by 9139
Abstract
Kraft pulp has to be bleached to eliminate the chromophoric structures, which cause a darkening of the pulp. In Nature, an equivalent role is assumed by ligninolytic enzymes such as lignin peroxidases, manganese peroxidases and laccases. The development of low molecular weight manganese [...] Read more.
Kraft pulp has to be bleached to eliminate the chromophoric structures, which cause a darkening of the pulp. In Nature, an equivalent role is assumed by ligninolytic enzymes such as lignin peroxidases, manganese peroxidases and laccases. The development of low molecular weight manganese peroxidase mimics may achieve environmentally-safe bleaching catalysts for the industry. Herein we report the synthesis and characterization of six manganese(III) complexes 1–6, incorporating dianionic hexadentate Schiff base ligands (H2L1-H2L4) and different anions. Complex 4, Mn2L22(H2O)2(DCA)2 was crystallographically characterized. Complexes 1–4 behave as more efficient mimics of peroxidase in contrast to 5–6. We have studied the use of these complexes as catalysts for the degradation of the lignin model compound veratryl alcohol. The biomimetic catalysts were used in conjunction with chlorine-free inexpensive co-oxidants as dioxygen or hydrogen peroxide. Yields up to 30% of veratryl alcohol conversion to veratraldehyde have been achieved at room temperature in presence of air flow using 0.5% of catalyst. Full article
(This article belongs to the Special Issue Biomimetic Catalysts)
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261 KiB  
Communication
Enzyme-Catalyzed Transetherification of Alkoxysilanes
by Vincenzo Abbate, Kurt F. Brandstadt, Peter G. Taylor and Alan R. Bassindale
Catalysts 2013, 3(1), 27-35; https://doi.org/10.3390/catal3010027 - 18 Jan 2013
Cited by 10 | Viewed by 9085
Abstract
We report the first evidence of an enzyme-catalyzed transetherification of model alkoxysilanes. During an extensive enzymatic screening in the search for new biocatalysts for silicon-oxygen bond formation, we found that certain enzymes promoted the transetherification of alkoxysilanes when tert-butanol or 1-octanol were [...] Read more.
We report the first evidence of an enzyme-catalyzed transetherification of model alkoxysilanes. During an extensive enzymatic screening in the search for new biocatalysts for silicon-oxygen bond formation, we found that certain enzymes promoted the transetherification of alkoxysilanes when tert-butanol or 1-octanol were used as the reaction solvents. Full article
(This article belongs to the Special Issue Biomimetic Catalysts)
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421 KiB  
Article
Advantages of the Biomimetic Nanostructured Films as an Immobilization Method vs. the Carbon Paste Classical Method
by Constantin Apetrei, Jose Antonio de Saja, Javier Zurro and Maria Luz Rodríguez-Méndez
Catalysts 2012, 2(4), 517-531; https://doi.org/10.3390/catal2040517 - 9 Nov 2012
Cited by 15 | Viewed by 6590
Abstract
Tyrosinase-based biosensors containing a phthalocyanine as electron mediator have been prepared by two different methods. In the first approach, the enzyme and the electron mediator have been immobilized in carbon paste electrodes. In the second method, they have been introduced in an arachidic [...] Read more.
Tyrosinase-based biosensors containing a phthalocyanine as electron mediator have been prepared by two different methods. In the first approach, the enzyme and the electron mediator have been immobilized in carbon paste electrodes. In the second method, they have been introduced in an arachidic acid Langmuir-Blodgett nanostructured film that provides a biomimetic environment. The sensing properties of non-nanostructured and nanostructured biosensors towards catechol, catechin and phenol have been analyzed and compared. The enzyme retains the biocatalytic properties in both matrixes. However, the nanostructured biomimetic films show higher values of maximum reaction rates and lowest apparent Michaelis-Menten constants. In both types of sensors, the sensitivity follows the decreasing order catechol > catechin > phenol. The detection limits observed are in the range of 1.8–5.4 μM for Langmuir-Blodgett biosensors and 8.19–8.57 μM for carbon paste biosensors. In summary, it has been demonstrated that the Langmuir-Blodgett films provide a biomimetic environment and nanostructured biosensors show better performances in terms of kinetic, detection limit and stability. Full article
(This article belongs to the Special Issue Biomimetic Catalysts)
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Review

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455 KiB  
Review
Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action
by Clemens K. Weiss and Katharina Landfester
Catalysts 2013, 3(2), 401-417; https://doi.org/10.3390/catal3020401 - 9 Apr 2013
Cited by 8 | Viewed by 7915
Abstract
Several important enzymatic reactions occurring in nature, such as, e.g., the digestion of fat, proceed only at the interface of two immiscible phases. Typically, these systems consist of an organic substrate, dispersed in an aqueous continuous phase, with a specialized enzyme capable of [...] Read more.
Several important enzymatic reactions occurring in nature, such as, e.g., the digestion of fat, proceed only at the interface of two immiscible phases. Typically, these systems consist of an organic substrate, dispersed in an aqueous continuous phase, with a specialized enzyme capable of working at the interface. For adopting such a system for organic synthesis, a stable heterophase system with a large interfacial area is required. These prerequisites can be found in so-called miniemulsions. Such liquid-liquid heterophase systems feature droplets with sizes smaller than 500 nm, and more importantly, these emulsions do not suffer from Ostwald ripening, as conventional emulsions do. Consequently, the droplets show long-term stability, even throughout reactions conducted in the droplets. In this review, we will briefly discuss the physicochemical background of miniemulsions, provide a comprehensive overview of the enzymatically catalyzed reactions conducted in miniemulsions and, as data are available, to compare the most important features to conventional systems, as reverse microemulsions, (macro)emulsions and solvent-based systems. Full article
(This article belongs to the Special Issue Biomimetic Catalysts)
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