Article
Chemistry, Physical
Lia Martinez-Montero, Dirk Tischler, Philipp Suess, Anett Schallmey, Maurice C. R. Franssen, Frank Hollmann, Caroline E. Paul
Summary: A biocatalytic cascade was developed for the synthesis of enantioenriched azido alcohols, introducing chiral substituents through enzymatic epoxidation and regioselective cleavage reactions, leading to highly enantioenriched aromatic azido alcohols. This approach demonstrates the potential for practical production of these chiral compounds using two-component flavoprotein monooxygenases.
CATALYSIS SCIENCE & TECHNOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Dominika Gyuranova, Radka Stadaniova, Zuzana Hegyi, Robert Fischer, Martin Rebros
Summary: Styrene monooxygenases are highly selective enzymes that can catalyze the epoxidation of alkenes with high enantioselectivity. The expression of two-component recombinant styrene monooxygenase in E. coli allows for the efficient preparation of chiral compounds containing oxirane rings.
Article
Biochemistry & Molecular Biology
Arne Matthews, Julia Schoenfelder, Simon Lagies, Erik Schleicher, Bernd Kammerer, Holly R. Ellis, Frederick Stull, Robin Teufel
Summary: The salvaging pathway encoded by the yxe operon in Bacillus subtilis has been identified for detoxification and utilization of S-(2-succino)-adducts. YxeK is characterized as an important enzyme in sulfur metabolism, potentially utilizing a noncanonical flavin-N5-peroxide mechanism for C-S bond oxygenolysis.
Article
Chemistry, Multidisciplinary
Sii Hong Lau, Meredith A. Borden, Talia J. Steiman, Lucy S. Wang, Marvin Parasram, Abigail G. Doyle
Summary: This study introduces a Ni/photoredox-catalyzed enantioselective reductive coupling of styrene oxides and aryl iodides, yielding enantioenriched 2,2-diarylalcohols. Analysis shows that enantioselectivity is correlated with the electronic properties of the ligands, with more electron-donating ligands leading to higher ee values. Experimental and computational studies support the hypothesis that reductive elimination is enantiodetermining and ligand electronic properties affect enantioselectivity by altering the position of the transition state structure.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Biochemistry & Molecular Biology
Stefania Bortolussi, Gianluca Catucci, Gianfranco Gilardi, Sheila J. Sadeghi
Summary: Human FMO3 enzyme is highly polymorphic, with variants demonstrating differences in substrate turnover rates. Studies on engineered proteins of common polymorphic variants show that the truncated, more soluble enzymes are better catalysts than full-length proteins. This suggests potential use of soluble enzyme forms for in vitro drug assays and biotechnological applications in high throughput systems.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
(2021)
Article
Engineering, Environmental
Zohre Kurt, Yi Qu, Jim C. Spain
Summary: A Rhodococcus sp. strain JS360 capable of biodegrading 4-nitroaniline (4NA) was isolated and its catabolic pathway was established. Enzyme assays and respirometry revealed that 4NA degradation involved monooxygenase-catalyzed reactions followed by ring cleavage. Sequencing and annotation of the genome identified candidate monooxygenases, which were cloned and expressed in E.coli. The heterologously expressed monooxygenases transformed 4NA to 4-aminophenol (4AP) and 4AP to 4-aminoresorcinol (4AR), revealing a novel pathway for nitroanilines and defining two monooxygenase mechanisms involved in the biodegradation of similar compounds.
JOURNAL OF HAZARDOUS MATERIALS
(2023)
Article
Chemistry, Organic
Robert Rollig, Caroline E. Paul, Magalie Claeys-Bruno, Katia Duquesne, Selin Kara, Veronique Alphand
Summary: This study demonstrates the independent functionality of the oxygenase in two-component flavoprotein monooxygenases and the mechanism of FMNH2 transport by free diffusion. It also highlights the importance of balancing FMN reduction and enzymatic (re)oxidation in a reductase-free system.
ORGANIC & BIOMOLECULAR CHEMISTRY
(2021)
Article
Microbiology
Andrew Willetts
Summary: Using purified enzymes, it was found that the isoenzymic 2,5- and 3,6-diketocamphane mono-oxygenases from Pseudomonas putida ATCC 17453 and the LuxAB luciferase from Vibrio fischeri ATCC 7744 are FMN-dependent two-component monooxygenases that promote redox coupling. Non-native flavin reductases from Escherichia coli ATCC 11105 and Aminobacter aminovorans ATCC 29600 were more efficient donors of FMNH2 compared to native flavin reductases for all three monooxygenases. These findings have potential practical implications for optimizing FMNH2-dependent biooxygenations of recognized practical and commercial value.
Article
Chemistry, Physical
Hu Xiao, Shuang Dong, Yan Liu, Xiao-Qiong Pei, Hui Lin, Zhong-Liu Wu
Summary: New (R)-selective styrene monooxygenases have been identified, showing high enantioselectivity in converting styrene analogues into (R)-epoxides with purity up to >99% ee. Site 46 was identified as a critical residue affecting the enantioselectivity of SMOs, providing a valuable green alternative for the synthesis of enantiopure (R)-epoxides.
CATALYSIS SCIENCE & TECHNOLOGY
(2021)
Review
Chemistry, Physical
Judith Muench, Pascal Puellmann, Wuyuan Zhang, Martin J. Weissenborn
Summary: The enzymatic hydroxylation of activated and nonactivated sp(3)-carbons is challenging in organic synthesis, but nature provides a variety of enzymes with catalytic versatility to tackle this task. Different enzymes have distinct specificity in substrate scope, selectivity, activity, stability, and catalytic cycle, and factors such as heterologous production, crystal structure availability, enzyme engineering potential, and substrate promiscuity play crucial roles in the applicability of these biocatalysts.
Article
Biochemistry & Molecular Biology
Robert Amongre, George Gassner
Summary: The study introduced an electroenzymatic method for epoxidation of styrene, utilizing a copper electrode for FAD reduction and a platinum electrode for oxygen generation, achieving a high conversion rate. This approach shows promise for other flavoprotein monooxygenases and may lead to advancements in quantitative transformation of styrene to styrene oxide.
BIOELECTROCHEMISTRY
(2021)
Article
Engineering, Environmental
Shu-Ting Zhang, Tao Li, Shi-Kai Deng, Jim C. Spain, Ning-Yi Zhou
Summary: This study reveals a novel bacterial metabolic pathway for the degradation of 4-nitroanisole, initiated by a three-component cytochrome P450 system (pnaABC). This system exhibits broad substrate specificity and can catalyze the degradation of nitroanisole derivatives.
JOURNAL OF HAZARDOUS MATERIALS
(2023)
Article
Biotechnology & Applied Microbiology
Shuang Dong, Donglin Fan, Qian Liu, Yinyin Meng, Xinyu Liu, Sen Yang, Hui Lin, Na Li, Hongge Chen
Summary: This study found that the monooxygenase HhMO from Herbaspirillum huttiense has excellent enantioselectivity and diastereoselectivity, and can catalyze the epoxidation reaction efficiently. The study also identified the important role of site 199 in the substrate access channel of HhMO in controlling enantioselectivity.
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
(2022)
Article
Biotechnology & Applied Microbiology
Leanne P. Sims, Colin W. J. Lockwood, Andrew T. Crombie, Justin M. Bradley, Nick E. Le Brun, J. Colin Murrell
Summary: Isoprene is a highly abundant climate-active gas and carbon source for some bacteria. Isoprene monooxygenase (IsoMO), a soluble diiron center monooxygenase, plays a crucial role in the bacterial degradation of isoprene, providing insights into the enzymatic basis for this process.
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
(2022)
Review
Biochemistry & Molecular Biology
Jiajing Li, Wenjing Gu, Zhongqiang Wang, Xiaojian Zhou, Yongzheng Chen
Summary: Optically active epoxides are important in the synthesis of pharmaceuticals, agricultural products, and fine chemicals. Researchers have developed various biocatalysts for the asymmetric epoxidation of unactive alkenes using eco-friendly and low-cost oxidants such as oxygen or hydrogen peroxide, providing better chemo-, regio-, and stereoselectivity under moderate reaction conditions. This paper reviews the advances, opportunities, and challenges of asymmetric epoxidation by biocatalysts.
