POM-supported metal carbonyl derivatives (PMCDs) represent a family of tremendous potential catalysts owing to their peculiar physical and chemical properties. Yet low-valence transition metal-substituted Dawson-type PMCD catalysts are uncommon. Hence, we synthesized a tricobalt-substituted PMCDs by conventional aqueous solution method, [Na(HO)](NH)[PWOCo(HO)(OH)Re(CO)]·13HO (), and characterized by single crystal X-ray diffraction crystallography, IR, and thermogravimetric analyses (TGA), etc. The obtained compound was employed as a catalyst for the oxidation of diphenylmethane (DPM) to benzophenone, giving 96.8% yield in the presence of -butyl hydroperoxide (TBHP) and pyridine. The control experiments indicate that Co metal ion plays an important role in the catalytic reactions. As a side note, the electrospray ionization mass spectrometry (ESI-MS) and UV spectroscopy showed that can retain its integrity in solution, and magnetic measurements indicated that exhibited a weaker ferromagnetic interaction at low temperature.
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http://dx.doi.org/10.1021/acs.inorgchem.0c00111 | DOI Listing |
ACS Chem Biol
October 2024
Department of Biocatalysis, Institute of Catalysis, CSIC, 28049 Madrid, Spain.
Fungal unspecific peroxygenases (UPOs) are gaining momentum in synthetic chemistry. Of special interest is the UPO from (UPO), which shows an exclusive repertoire of oxyfunctionalizations, including the terminal hydroxylation of alkanes, the α-oxidation of fatty acids and the C-C cleavage of corticosteroids. However, the lack of heterologous expression systems to perform directed evolution has impeded its engineering for practical applications.
View Article and Find Full Text PDFBiol Chem
September 2024
Microbial Biotechnology, Faculty of Biology and Biotechnology, 9142 Ruhr University Bochum, D-44801 Bochum, Germany.
Cytochrome P450 monooxygenases are recognized as versatile biocatalysts due to their broad reaction capabilities. One important reaction is the hydroxylation of non-activated C-H bonds. The subfamily CYP153A is known for terminal hydroxylation reactions, giving access to functionalized aliphatics.
View Article and Find Full Text PDFFaraday Discuss
September 2024
CAS Key Laboratory of Biofuels and Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China.
Cytochrome P450 monooxygenases (P450s) are well recognized as versatile bio-oxidation catalysts. However, the catalytic functions of P450s are highly dependent on NAD(P)H and redox partner proteins. Our group has recently reported the use of a dual-functional small molecule (DFSM) for generating peroxygenase activity of P450BM3, a long-chain fatty acid hydroxylase from .
View Article and Find Full Text PDFChembiochem
October 2024
Ruhr-University Bochum, Faculty of Biology and Biotechnology, Microbial Biotechnology, Universitätsstraße 150, 44780, Bochum, Germany.
Cytochrome P450 monooxygenases (CYPs) are valuable biocatalysts for the oxyfunctionalization of non-activated carbon-hydrogen bonds. Most CYPs rely on electron transport proteins as redox partners. In this study, the ferredoxin reductase (FdR) and ferredoxin (FD) for a cytochrome P450 monooxygenase from Acinetobacter sp.
View Article and Find Full Text PDFAcc Chem Res
January 2024
CAS Key Laboratory of Biofuels and Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China.
ConspectusCytochrome P450 monooxygenase is a versatile oxidizing enzyme with great potential in synthetic chemistry and biology. However, the dependence of its catalytic function on the nicotinamide cofactor NAD(P)H and redox partner proteins limits the practical catalytic application of P450 . An alternative to expensive cofactors is low-cost HO, which can be used directly to exploit the catalytic potential of P450s.
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