Nature's enzymes are an ongoing source of inspiration for scientists. The complex processes behind their selectivity and efficiency is slowly being unraveled, and these findings have spawned many biomimetic catalysts. However, nearly all focus on the conversion of small molecular substrates. Nature itself is replete with inventive catalytic systems which modify, replicate, or decompose entire polymers, often in a processive fashion. Such processivity can, for example, enhance the rate of catalysis by clamping to the polymer substrate, which imparts a large effective molarity. Reviewed herein are the various strategies for processivity in nature's arsenal and their properties. An overview of what has been achieved by chemists aiming to mimic one of nature's greatest tricks is also included.
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http://dx.doi.org/10.1002/anie.201404848 | DOI Listing |
Virologie (Montrouge)
December 2024
Unité des Virus émergents (UVE : Aix-Marseille Univ, Università di Corsica, Corte, IRD 190, Inserm 1207, IRBA), France.
The reverse transcriptase of Moloney Murine Leukemia Virus (MMLV) is an enzyme that synthesizes DNA from an RNA template. Among reverse transcriptases, this enzyme is currently the most commonly used in molecular biology and diagnostics. Since its discovery, this viral protein has been extensively studied, shedding light on its structural and functional characteristics, and offering opportunities to optimize the catalytic performances for biotechnological applications.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
December 2024
Hubei Research Center of Fundamental Science-Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, 430072, China.
The "Magic Methyl" effect has received tremendous interest in medicinal chemistry due to the significant pharmacological and physical modification of properties that have been observed upon introducing a methyl group, especially, a stereogenic methyl group into potential chiral drug candidates. The prevalence of stereogenic β-methyl ketone structural motifs in bioactive compounds and natural products has long motivated the development of enantioselective strategies toward their synthesis. Herein, we have rationally designed a Rh-catalyzed asymmetric monohydrogenation of readily-available β'-methylene conjugated enones with high efficiency and remarkable site-selectivity and enantioselectivity control for the practical construction of enantioenriched β'-methyl unsaturated enones that are difficult to access by other methods.
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk 630090, Russia.
The mechanism of transcription proceeds through the formation of R-loop structures containing a DNA-RNA heteroduplex and a single-stranded DNA segment that should be placed inside the elongation complex; therefore, these nucleic acid segments are limited in length. The attachment of each nucleotide to the 3' end of an RNA strand requires a repeating cycle of incoming nucleoside triphosphate binding, catalysis, and enzyme translocation. Within these steps of transcription elongation, RNA polymerase sequentially goes through several states and is post-translocated, catalytic, and pre-translocated.
View Article and Find Full Text PDFNature
December 2024
Single Molecule Biophysics Group, MRC Laboratory of Medical Sciences, London, UK.
The yeast SWR1 complex catalyses the exchange of histone H2A-H2B dimers in nucleosomes, with Htz1-H2B dimers. Here we used single-molecule analysis to demonstrate two-step double exchange of the two H2A-H2B dimers in a canonical yeast nucleosome with Htz1-H2B dimers, and showed that double exchange can be processive without release of the nucleosome from the SWR1 complex. Further analysis showed that bound nucleosomes flip between two states, with each presenting a different face, and hence histone dimer, to SWR1.
View Article and Find Full Text PDFInt J Mol Sci
August 2024
Department of Chemistry, University of Texas at San Antonio, San Antonio, TX 78249, USA.
Cytochrome P450 (P450) enzymes dominate steroid metabolism. In general, the simple C-hydroxylation reactions are mechanistically straightforward and are generally agreed to involve a perferryl oxygen species (formally FeO). Several of the steroid transformations are more complex and involve C-C bond scission.
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