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Article ; Online: Photoexcited Enzymes for Asymmetric Csp

Schmidt, Sandy

Angewandte Chemie (International ed. in English)

2022 Volume 61, Issue 52, Page(s) e202214313

Abstract: Enzymes have several advantages over conventional catalysts for organic synthesis. Over the last two decades, much effort has been made to further extend the scope of biocatalytic reactions available to synthetic chemists, particularly by expanding the ... ...

Abstract	Enzymes have several advantages over conventional catalysts for organic synthesis. Over the last two decades, much effort has been made to further extend the scope of biocatalytic reactions available to synthetic chemists, particularly by expanding the repertoire of enzymes for abiological transformations. In this regard, exciting new developments in the area of photobiocatalysis enable now the introduction of non-natural reactivity in enzymes to solve long-standing synthetic challenges. A recently described example from the Hyster group demonstrates in an unprecedented way how the combination of photochemistry with enzyme catalysis empowers the catalytic asymmetric construction of Csp
MeSH term(s)	Stereoisomerism ; Catalysis ; Biocatalysis ; Chemistry Techniques, Synthetic ; Photochemistry ; Enzymes/metabolism
Chemical Substances	Enzymes
Language	English
Publishing date	2022-11-10
Publishing country	Germany
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202214313
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Article ; Online: Cell-free chemoenzymatic cascades with bio-based molecules.

Terholsen, Henrik / Schmidt, Sandy

Current opinion in biotechnology

2023 Volume 85, Page(s) 103058

Abstract: For the valorization of various bio-based feedstocks, the combination of different catalytic systems with biocatalysis in chemoenzymatic cascades has been shown to have high potential. However, the development of such integrated catalytic systems is ... ...

Abstract	For the valorization of various bio-based feedstocks, the combination of different catalytic systems with biocatalysis in chemoenzymatic cascades has been shown to have high potential. However, the development of such integrated catalytic systems is often limited by catalyst incompatibility. Therefore, incorporating novel catalytic concepts into the chemoenzymatic valorization of bio-based feedstocks is currently of great interest. This article provides an overview of the methods/approaches used to advance the development of chemoenzymatic cascades for the catalytic upgrading of bio-based feedstocks. It specifically focuses on recent developments in the combination of enzymes with organo- and chemocatalysis. Furthermore, current applications and future perspectives of integrating novel catalytic systems such as photo- and electrocatalysis toward new synthetic routes for the utilization of the often highly functionalized bio-based compounds are reviewed.
MeSH term(s)	Biocatalysis ; Catalysis
Language	English
Publishing date	2023-12-27
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1052045-4
ISSN	1879-0429 ; 0958-1669
ISSN (online)	1879-0429
ISSN	0958-1669
DOI	10.1016/j.copbio.2023.103058
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Article ; Online: Rieske Oxygenases and Other Ferredoxin-Dependent Enzymes: Electron Transfer Principles and Catalytic Capabilities.

Runda, Michael E / de Kok, Niels A W / Schmidt, Sandy

Chembiochem : a European journal of chemical biology

2023 Volume 24, Issue 15, Page(s) e202300078

Abstract: Enzymes that depend on sophisticated electron transfer via ferredoxins (Fds) exhibit outstanding catalytic capabilities, but despite decades of research, many of them are still not well understood or exploited for synthetic applications. This review aims ...

Abstract	Enzymes that depend on sophisticated electron transfer via ferredoxins (Fds) exhibit outstanding catalytic capabilities, but despite decades of research, many of them are still not well understood or exploited for synthetic applications. This review aims to provide a general overview of the most important Fd-dependent enzymes and the electron transfer processes involved. While several examples are discussed, we focus in particular on the family of Rieske non-heme iron-dependent oxygenases (ROs). In addition to illustrating their electron transfer principles and catalytic potential, the current state of knowledge on structure-function relationships and the mode of interaction between the redox partner proteins is reviewed. Moreover, we highlight several key catalyzed transformations, but also take a deeper dive into their engineerability for biocatalytic applications. The overall findings from these case studies highlight the catalytic capabilities of these biocatalysts and could stimulate future interest in developing additional Fd-dependent enzyme classes for synthetic applications.
MeSH term(s)	Oxygenases/metabolism ; Ferredoxins/metabolism ; Electrons ; Models, Molecular ; Electron Transport ; Catalysis
Chemical Substances	Oxygenases (EC 1.13.-) ; Ferredoxins
Language	English
Publishing date	2023-06-21
Publishing country	Germany
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202300078
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Article ; Online: Enzymatic Oxy- and Amino-Functionalization in Biocatalytic Cascade Synthesis: Recent Advances and Future Perspectives.

Grandi, Eleonora / Feyza Özgen, Fatma / Schmidt, Sandy / Poelarends, Gerrit J

Angewandte Chemie (International ed. in English)

2023 Volume 62, Issue 48, Page(s) e202309012

Abstract: Biocatalytic cascades are a powerful tool for building complex molecules containing oxygen and nitrogen functionalities. Moreover, the combination of multiple enzymes in one pot offers the possibility to minimize downstream processing and waste ... ...

Abstract	Biocatalytic cascades are a powerful tool for building complex molecules containing oxygen and nitrogen functionalities. Moreover, the combination of multiple enzymes in one pot offers the possibility to minimize downstream processing and waste production. In this review, we illustrate various recent efforts in the development of multi-step syntheses involving C-O and C-N bond-forming enzymes to produce high value-added compounds, such as pharmaceuticals and polymer precursors. Both in vitro and in vivo examples are discussed, revealing the respective advantages and drawbacks. The use of engineered enzymes to boost the cascades outcome is also addressed and current co-substrate and cofactor recycling strategies are presented, highlighting the importance of atom economy. Finally, tools to overcome current challenges for multi-enzymatic oxy- and amino-functionalization reactions are discussed, including flow systems with immobilized biocatalysts and cascades in confined nanomaterials.
MeSH term(s)	Enzymes, Immobilized ; Biocatalysis
Chemical Substances	Enzymes, Immobilized
Language	English
Publishing date	2023-09-12
Publishing country	Germany
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202309012
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Article: Baeyer-Villiger monooxygenases: From protein engineering to biocatalytic applications.

Schmidt, Sandy / Bornscheuer, Uwe T

The Enzymes

2020 Volume 47, Page(s) 231–281

Abstract: Biocatalytic processes are well established for the synthesis of high-value fine chemicals, especially for chiral pharmaceutical intermediates, by using natural or engineered enzymes. In contrast, examples for the enzymatic synthesis of bulk chemicals ... ...

Abstract	Biocatalytic processes are well established for the synthesis of high-value fine chemicals, especially for chiral pharmaceutical intermediates, by using natural or engineered enzymes. In contrast, examples for the enzymatic synthesis of bulk chemicals are still rare. Especially for the synthesis of polymer precursors such as ɛ-caprolactone, that is still produced under harsh conditions by using peracetic acid, Baeyer-Villiger monooxygenases (BVMOs) represent promising alternative catalysts that can perform the reaction under mild conditions. However, industrial production of this bulk chemical using a biocatalyst such as a BVMO has not been achieved yet due to a number of reasons. In this book chapter, we are emphasizing the versatility of BVMOs and their catalyzed reactions, and address several examples where protein engineering was applied in order to overcome several limitations associated to the use of BVMOs. Finally, we highlight several examples of BVMO applications, either in single enzyme transformations, or BVMOs involved in cascade reactions. By mainly focusing on recent developments and achievements in the field, we outline different concepts that were developed in order to pave the way for an industrial application of BVMOs.
MeSH term(s)	Biocatalysis ; Mixed Function Oxygenases/chemistry ; Oxidation-Reduction ; Protein Engineering
Chemical Substances	Mixed Function Oxygenases (EC 1.-)
Language	English
Publishing date	2020-07-18
Publishing country	United States
Document type	Journal Article
ISSN	0423-2607
ISSN	0423-2607
DOI	10.1016/bs.enz.2020.05.007
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Book ; Online ; Thesis: An artificial enzyme cascade for the biocatalytic synthesis of polymer building blocks

Schmidt, Sandy

2015

Abstract: Enzymkatalyse, Cyclohexanon-Monooxygenase, Caprolacton ... , Polycaprolactone, Lipase ... In this thesis an artificial enzyme cascade consisting of an ADH from Lactobacillus kefir, a CHMO from Acinetobacter sp. NCIMB 9871 and lipase A from Candida ... ...

Author's details	von Sandy Schmidt
Abstract	Enzymkatalyse, Cyclohexanon-Monooxygenase, Caprolacton <epsilon->, Polycaprolactone, Lipase In this thesis an artificial enzyme cascade consisting of an ADH from Lactobacillus kefir, a CHMO from Acinetobacter sp. NCIMB 9871 and lipase A from Candida antarctica has been investigated for the biocatalytic synthesis of the bulk chemical e-caprolactone as well as several derivatives for their direct utilization as polymer building blocks. Due to major limitations, which hamper such a biocatalytic route, the first addressed demand in this work was the improvement of the stability of the CHMO. By structure-guided engineering, distinctively improved variants concerning the resistance against oxidation as well as temperature stability without compromising the catalytic activity were successfully created. Due to the incomplete knowledge of the mechanisms that lead to thermal and/or oxidative inactivation of enzymes, this study illustrates that the selection of mutations for increased protein stability is still hard to predict. Thus, these results can serve as a basis for further stability studies on this enzyme class to give better insights into the underlying mechanisms, which determine the stability of an enzyme. Such a highly stabilized biocatalyst will pave the way for the successful use of flavin-dependent enzymes for industrial applications. A further aim of this thesis was dedicated to the second major hurdle en route to polyester precursors represented by the product inhibition and enzyme deactivation caused by e-caprolactone, particularly at higher concentrations ...
Language	English
Size	Online-Ressource (PDF-Datei: 145 S., 37011 KB), Ill., graph. Darst.
Publisher	Universitätsbibliothek
Publishing place	Greifswald
Document type	Book ; Online ; Thesis
Thesis / German Habilitation thesis	Univ., Diss.--Greifswald, 2015
Database	Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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Article ; Online: Photo-biocatalytic Cascades: Combining Chemical and Enzymatic Transformations Fueled by Light.

Özgen, Fatma Feyza / Runda, Michael E / Schmidt, Sandy

Chembiochem : a European journal of chemical biology

2020 Volume 22, Issue 5, Page(s) 790–806

Abstract: In the field of green chemistry, light - an attractive natural agent - has received particular attention for driving biocatalytic reactions. Moreover, the implementation of light to drive (chemo)enzymatic cascade reactions opens up a golden window of ... ...

Abstract	In the field of green chemistry, light - an attractive natural agent - has received particular attention for driving biocatalytic reactions. Moreover, the implementation of light to drive (chemo)enzymatic cascade reactions opens up a golden window of opportunities. However, there are limitations to many current examples, mostly associated with incompatibility between the enzyme and the photocatalyst. Additionally, the formation of reactive radicals upon illumination and the loss of catalytic activities in the presence of required additives are common observations. As outlined in this review, the main question is how to overcome current challenges to the exploitation of light to drive (chemo)enzymatic transformations. First, we highlight general concepts in photo-biocatalysis, then give various examples of photo-chemoenzymatic (PCE) cascades, further summarize current synthetic examples of PCE cascades and discuss strategies to address the limitations.
MeSH term(s)	Animals ; Biocatalysis ; Enzymes/chemistry ; Enzymes/metabolism ; Humans ; Light ; Photochemical Processes ; Protein Engineering
Chemical Substances	Enzymes
Language	English
Publishing date	2020-11-06
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202000587
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Article ; Online: Overcoming the Incompatibility Challenge in Chemoenzymatic and Multi-Catalytic Cascade Reactions.

Schmidt, Sandy / Castiglione, Kathrin / Kourist, Robert

Chemistry (Weinheim an der Bergstrasse, Germany)

2017

Abstract: Multi-catalytic cascade reactions bear a great potential to minimize downstream and purification steps, leading to a drastic reduction of the produced waste. In many examples, the compatibility of chemo- and biocatalytic steps could be easily achieved. ... ...

Abstract	Multi-catalytic cascade reactions bear a great potential to minimize downstream and purification steps, leading to a drastic reduction of the produced waste. In many examples, the compatibility of chemo- and biocatalytic steps could be easily achieved. Problems associated with the incompatibility of the catalysts and their reactions, however, are very frequent. Cascade-like reactions can hardly occur in this way. One possible solution to combine, in principle, incompatible chemo- and biocatalytic reactions is the defined control of the microenvironment by compartmentalization or scaffolding. Current methods for the control of the microenvironment of biocatalysts go far beyond classical enzyme immobilization and are thus believed to be very promising tools to overcome incompatibility issues and to facilitate the synthetic application of cascade reactions. In this Minireview, we will summarize recent synthetic examples of (chemo)enzymatic cascade reactions and outline promising methods for their spatial control either by using bio-derived or synthetic systems.
Language	English
Publishing date	2017-09-06
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1478547-x
ISSN	1521-3765 ; 0947-6539
ISSN (online)	1521-3765
ISSN	0947-6539
DOI	10.1002/chem.201703353
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Article ; Online: Library Growth and Protein Expression: Optimal and Reproducible Microtiter Plate Expression of Recombinant Enzymes in E. coli Using MTP Shakers.

Schmidt, Sandy / Dörr, Mark / Bornscheuer, Uwe T

Methods in molecular biology (Clifton, N.J.)

2017 Volume 1685, Page(s) 145–156

Abstract: Escherichia coli (E. coli) as heterologous host enables the recombinant expression of the desired protein in high amounts. Nevertheless, the expression in such a host, especially by utilizing a strong induction system, can result in insoluble and/or ... ...

Abstract	Escherichia coli (E. coli) as heterologous host enables the recombinant expression of the desired protein in high amounts. Nevertheless, the expression in such a host, especially by utilizing a strong induction system, can result in insoluble and/or inactive protein fractions (inclusion bodies). Furthermore, the expression of different enzyme variants often leads to a diverse growth behavior of the E. coli clones resulting in the identification of false-positives when screening a mutant library. Thus, we developed a protocol for an optimal and reproducible protein expression in microtiter plates showcased for the expression of the cyclohexanone monooxygenase (CHMO) from Acinetobacter sp. NCIMB 9871. By emerging this protocol, several parameters concerning the expression medium, the cultivation temperatures, shaking conditions as well as time and induction periods for CHMO were investigated. We employed a microtiter plate shaker with humidity and temperature control (Cytomat™) (integrated in a robotic platform) to obtain an even growth and expression over the plates. Our optimized protocol provides a comprehensive overview of the key factors influencing a reproducible protein expression and this should serve as basis for the adaptation to other enzyme classes.
MeSH term(s)	Acinetobacter/enzymology ; Acinetobacter/genetics ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Batch Cell Culture Techniques/instrumentation ; Escherichia coli/genetics ; Escherichia coli/growth & development ; Gene Expression ; Gene Library ; Oxygenases/genetics ; Oxygenases/metabolism ; Protein Engineering ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Chemical Substances	Bacterial Proteins ; Recombinant Proteins ; Oxygenases (EC 1.13.-) ; cyclohexanone oxygenase (EC 1.14.13.-)
Language	English
Publishing date	2017-10-30
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7366-8_8
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Hydrogen-Driven Cofactor Regeneration for Stereoselective Whole-Cell C=C Bond Reduction in Cupriavidus necator.

Assil-Companioni, Leen / Schmidt, Sandy / Heidinger, Petra / Schwab, Helmut / Kourist, Robert

ChemSusChem

2019 Volume 12, Issue 11, Page(s) 2361–2365

Abstract: The coupling of recombinantly expressed oxidoreductases to endogenous hydrogenases for cofactor recycling permits the omission of organic cosubstrates as sacrificial electron donors in whole-cell biotransformations. This increases atom efficiency and ... ...

Abstract	The coupling of recombinantly expressed oxidoreductases to endogenous hydrogenases for cofactor recycling permits the omission of organic cosubstrates as sacrificial electron donors in whole-cell biotransformations. This increases atom efficiency and simplifies the reaction. A recombinant ene-reductase was expressed in the hydrogen-oxidizing proteobacterium Cupriavidus necator H16. In hydrogen-driven biotransformations, whole cells catalyzed asymmetric C=C bond reduction of unsaturated cyclic ketones with stereoselectivities up to >99 % enantiomeric excess. The use of hydrogen as a substrate for growth and cofactor regeneration is particularly attractive because it represents a strategy for improving atom efficiency and reducing side product formation associated with the recycling of organic cofactors.
MeSH term(s)	Bacterial Proteins/metabolism ; Biotransformation ; Carbon/metabolism ; Cupriavidus necator/metabolism ; Electrons ; Hydrogen/metabolism
Chemical Substances	Bacterial Proteins ; Carbon (7440-44-0) ; Hydrogen (7YNJ3PO35Z)
Language	English
Publishing date	2019-04-29
Publishing country	Germany
Document type	Journal Article
ISSN	1864-564X
ISSN (online)	1864-564X
DOI	10.1002/cssc.201900327
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