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Related Concept Videos

Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
Colors and Magnetism03:02

Colors and Magnetism

Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human eye.

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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Published on: December 4, 2017

Structure-function study of peroxidase-like G-quadruplex-hemin complexes.

De-Ming Kong1, Wei Yang, Jing Wu

  • 1Key Laboratory of Functional Polymer Materials, Ministry of Education, Nankai University, Tianjin, 300071, People's Republic of China. kongdem@nankai.edu.cn

The Analyst
|January 26, 2010
PubMed
Summary
This summary is machine-generated.

G-quadruplex-hemin complexes exhibit peroxidase activity, with parallel structures showing significantly higher activity than antiparallel ones. Hemin addition influences G-quadruplex folding, impacting catalytic function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Supramolecular Chemistry

Background:

  • G-quadruplexes are nucleic acid structures with diverse biological roles.
  • Hemin, an iron-containing porphyrin, can form complexes with G-quadruplexes.
  • These complexes can exhibit catalytic (peroxidase) activity.

Purpose of the Study:

  • To investigate the structure-function relationship of G-quadruplex-hemin complexes.
  • To correlate G-quadruplex folding with peroxidase activity.
  • To understand how hemin influences G-quadruplex structure and function.

Main Methods:

  • Synthesis and characterization of 22 distinct G-quadruplex oligonucleotides.
  • Peroxidase activity assays.
  • Circular dichroism (CD) spectroscopy to determine G-quadruplex structure (parallel vs. antiparallel).

Main Results:

  • Hemin addition can induce structural transitions in G-quadruplexes (e.g., antiparallel to parallel).
  • G-quadruplex formation is essential for observed peroxidase activity.
  • Parallel G-quadruplex-hemin complexes display substantially higher peroxidase activity compared to antiparallel ones.

Conclusions:

  • The structural conformation of G-quadruplexes is a critical determinant of their peroxidase activity in hemin complexes.
  • Parallel G-quadruplexes are superior scaffolds for hemin-based peroxidase mimetics.
  • Hemin plays a dual role in complex formation: influencing structure and enabling catalysis.