Stabilization of Reactive Intermediates and Transition States in Enzyme Active Sites by Hydrogen Bonding

Gerlt, J.A.

doi:10.1016/b978-0-08-091283-7.00131-4

Cited by 5 publications

(3 citation statements)

References 87 publications

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“…Sahin and co-authors published the synthesis of magnetic nanoparticles coated with polyvinyl alcohol and trypsin covalent immobilization on their surface with glutaraldehyde as a linker [134]. Trypsin is hydrolase that selectively catalyzes the hydrolysis of peptide bonds [135]. According to the published results, immobilized trypsin showed at 40 • C greater stability than the free enzyme.…”

Section: Immobilization Of Proteins On Nanoparticles Coated With Poly...mentioning

confidence: 99%

Metal and Metal Oxide Nanoparticles: Design, Characterization, and Biomedical Applications

2022

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Section: Immobilization Of Proteins On Nanoparticles Coated With Poly...mentioning

confidence: 99%

Metal and Metal Oxide Nanoparticles: Design, Characterization, and Biomedical Applications

2022

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“…Sahin and co-authors published the synthesis of magnetic nanoparticles coated with polyvinyl alcohol and trypsin covalent immobilization on their surface with glutaraldehyde as a linker [ 134 ]. Trypsin is hydrolase that selectively catalyzes the hydrolysis of peptide bonds [ 135 ]. According to the published results, immobilized trypsin showed at 40 °C greater stability than the free enzyme.…”

Section: Immobilization Of Proteins On Polymer-coated Nanoparticlementioning

confidence: 99%

Polymer-Coated Magnetite Nanoparticles for Protein Immobilization

et al. 2021

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Since their discovery, magnetic nanoparticles (MNPs) have become materials with great potential, especially considering the applications of biomedical sciences. A series of works on the preparation, characterization, and application of MNPs has shown that the biological activity of such materials depends on their size, shape, core, and shell nature. Some of the most commonly used MNPs are those based on a magnetite core. On the other hand, synthetic biopolymers are used as a protective surface coating for these nanoparticles. This review describes the advances in the field of polymer-coated MNPs for protein immobilization over the past decade. General methods of MNP preparation and protein immobilization are presented. The most extensive section of this article discusses the latest work on the use of polymer-coated MNPs for the physical and chemical immobilization of three types of proteins: enzymes, antibodies, and serum proteins. Where possible, the effectiveness of the immobilization and the activity and use of the immobilized protein are reported. Finally, the information available in the peer-reviewed literature and the application perspectives for the MNP-immobilized protein systems are summarized as well.

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“…It is generally assumed that during glycolysis, a metabolic reaction chain shared by nearly all organisms on Earth, ambient-water H is incorporated into the C-bonded H fraction which includes de novo formation of C–H bonds. − During the fifth step of the glycolysis, an H atom from ambient water is newly bound to the C 2 position of the glycerinealdehyde-3-phosphate (GAP) molecule. This H atom is eventually conserved in bacterial biomass if pyruvate as the end-product of glycolysis enters the anabolic mode of the tricarboxylic acid (TCA) cycle that generates biosynthesis products.…”

Section: Introductionmentioning

confidence: 99%

Incorporation of Ambient Water-H into the C-Bonded H Pool of Bacteria during Substrate-Specific Metabolism

Kessler

Merseburger

Kappler

et al. 2022

ACS Earth Space Chem.

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The stable isotope ratios of C-bonded H (δ2Hn values) can be used to locate soil samples for forensic purposes because of their close correlation with the δ2H values of precipitation. Post-sampling bacterial activity might change the δ2Hn values via glycolysis. We tested to which degree C-bonded H is replaced by H from ambient water under favorable and unfavorable growing conditions. We provided two heterotrophic bacteria (Bacillus atrophaeus, Escherichia coli) with glucose (favorable) or lysine (unfavorable) under aerobic conditions. We assessed the H incorporation from ambient water via 2H labeling. We found that the H incorporation into bacterial biomass in the glucose treatment was 79 ± 5.9% (B. atrophaeus) and 43 ± 3.0% (E. coli), likely as a consequence of glycolysis and conservation of the δ2H value in the anabolic mode of the tricarboxylic acid (TCA) cycle. Differences between species were possibly related with different compositions of metabolite mixtures. The bacteria did hardly grow with lysine while respiration continued, and we found no H incorporation because the catabolic mode of the TCA cycle, which was active when the bacteria grew on lysine, is associated with CO2 release and a complete cleavage of former C–2H bonds. Our results support the glycolysis pathway as a mechanism underlying the incorporation of ambient-water H into the C-bonded H pool of bacteria. Stressful conditions forcing bacteria into a catabolism-dominated metabolism disable the incorporation of ambient-water H, and δ2Hn values can be applied to identify the origin of soil samples in forensics.

show abstract

Stabilization of Reactive Intermediates and Transition States in Enzyme Active Sites by Hydrogen Bonding

Cited by 5 publications

References 87 publications

Metal and Metal Oxide Nanoparticles: Design, Characterization, and Biomedical Applications

Metal and Metal Oxide Nanoparticles: Design, Characterization, and Biomedical Applications

Polymer-Coated Magnetite Nanoparticles for Protein Immobilization

Incorporation of Ambient Water-H into the C-Bonded H Pool of Bacteria during Substrate-Specific Metabolism

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