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Related Concept Videos

Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
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Catalytically Perfect Enzymes01:07

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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
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Reduction of Alkenes: Catalytic Hydrogenation02:13

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Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
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Reduction of Benzene to Cyclohexane: Catalytic Hydrogenation01:28

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Unlike the easy catalytic hydrogenation of an alkene double bond, hydrogenation of a benzene double bond under similar reaction conditions does not take place easily. For example, in the reduction of stilbene, the benzene ring remains unaffected while the alkene bond gets reduced. Hydrogenation of an alkene double bond is exothermic and a favorable process. In contrast, to hydrogenate the first unsaturated bond of benzene, an energy input is needed; that is, the process is endothermic. This is...
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Molecular Models02:00

Molecular Models

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Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
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Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
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Fragmenting Bulk Hydrogels and Processing into Granular Hydrogels for Biomedical Applications
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Logic Catalytic Interconversion of G-Molecular Hydrogel.

Ruibo Zhong1,2, Mingshu Xiao1, Changfeng Zhu

  • 1Shanghai Key Laboratory of Green Chemistry and Chemical Processes, School of Chemistry and Molecular Engineering, East China Normal University , 500 Dongchuan Road, Shanghai 200241, P. R. China.

ACS Applied Materials & Interfaces
|January 17, 2018
PubMed
Summary

This study introduces an artificial enzyme hydrogel (AEH) for highly sensitive lead (Pb2+) detection. The AEH system leverages G-quadruplex (G4) stabilization changes to achieve precise Pb2+ sensing and biomolecular computation.

Keywords:
G-quadruplexPb2+ detectionartificial enzyme hydrogelcatalytic interconversionlogic gate

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Area of Science:

  • Biomolecular Engineering
  • Nanomaterials
  • Chemical Sensing

Background:

  • G-quadruplex (G4) structures are crucial in biological processes and have been explored for biosensing applications.
  • Developing sensitive and selective methods for detecting heavy metal ions like lead (Pb2+) is critical for environmental and health monitoring.
  • Artificial enzyme hydrogels (AEHs) offer a promising platform for developing novel biosensing systems.

Purpose of the Study:

  • To construct an artificial enzyme hydrogel (AEH) system for sensitive and selective detection of lead ions (Pb2+).
  • To investigate the mechanism of Pb2+-induced conformational changes and activity loss in the AEH.
  • To explore the potential of the AEH system for biomolecular computation.

Main Methods:

  • Cation-templated self-assembly of guanosine and KB(OH)4 to incorporate hemin into G-quadruplex (G4) structures, forming an AEH.
  • Utilizing the differential stabilization of G4 by Pb2+ versus K+ to trigger hemin release and loss of enzyme activity.
  • Characterizing the AEH response to varying concentrations of Pb2+ and other metal ions.

Main Results:

  • The AEH system demonstrated highly sensitive and selective detection of Pb2+ within a range of 1 pM to 50 nM, with a limit of detection of approximately 0.32 pM.
  • Pb2+ ions were found to be more efficient than K+ in stabilizing G4, leading to Pb2+-induced hemin release and loss of AEH activity.
  • The system exhibited high selectivity for Pb2+ over other tested metal ions and was successfully used to construct two-input INHIBIT logic gates.

Conclusions:

  • The developed AEH-based system provides a novel and effective platform for the ultrasensitive and selective detection of Pb2+.
  • The Pb2+-induced catalytic interconversion mechanism offers a robust sensing strategy with a significantly lower detection limit compared to previous G4-DNAzyme methods.
  • The AEH system's versatility opens new avenues for advanced sensing applications and biomolecular computation.