Special Issue "Biomimetic Catalysts"

Quicklinks

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

Deadline for manuscript submissions: closed (15 January 2013)

Special Issue Editor

Guest Editor
Prof. Dr. Armando Córdova

1Department 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
Website | E-Mail
Fax: +46 8 154908
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

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed Open Access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1000 CHF (Swiss Francs).

Keywords

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

Published Papers (4 papers)

View options order results:
result details:
Displaying articles 1-4
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle Biomimetic Catalysts for Oxidation of Veratryl Alcohol, a Lignin Model Compound
Catalysts 2013, 3(1), 232-246; doi:10.3390/catal3010232
Received: 21 December 2012 / Revised: 8 February 2013 / Accepted: 17 February 2013 / Published: 4 March 2013
Cited by 3 | PDF Full-text (316 KB) | HTML Full-text | XML Full-text
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 16, incorporating dianionic hexadentate Schiff base ligands (H2L1-H2L4) and different anions. Complex 4, Mn2L22(H2O)2(DCA)2 was crystallographically characterized. Complexes 14 behave as more efficient mimics of peroxidase in contrast to 56. 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)
Open AccessCommunication Enzyme-Catalyzed Transetherification of Alkoxysilanes
Catalysts 2013, 3(1), 27-35; doi:10.3390/catal3010027
Received: 27 November 2012 / Revised: 20 December 2012 / Accepted: 8 January 2013 / Published: 18 January 2013
Cited by 2 | PDF Full-text (261 KB) | HTML Full-text | XML Full-text
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)
Figures

Open AccessArticle Advantages of the Biomimetic Nanostructured Films as an Immobilization Method vs. the Carbon Paste Classical Method
Catalysts 2012, 2(4), 517-531; doi:10.3390/catal2040517
Received: 27 September 2012 / Revised: 26 October 2012 / Accepted: 1 November 2012 / Published: 9 November 2012
Cited by 4 | PDF Full-text (421 KB) | HTML Full-text | XML Full-text
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)

Review

Jump to: Research

Open AccessReview Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action
Catalysts 2013, 3(2), 401-417; doi:10.3390/catal3020401
Received: 18 January 2013 / Revised: 11 March 2013 / Accepted: 26 March 2013 / Published: 9 April 2013
Cited by 2 | PDF Full-text (455 KB) | HTML Full-text | XML Full-text
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)

Journal Contact

MDPI AG
Catalysts Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
catalysts@mdpi.com
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
Editorial Board
Contact Details Submit to Catalysts
Back to Top