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Related Concept Videos

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...
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Pedigree Analysis

Overview
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...
Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

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Related Experiment Video

Updated: Jul 6, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Tetrahydrobiopterin.

Muhiddin A Ozkor1, Arshed A Quyyumi

  • 1Emory University, 1364 Clifton Road NE, Suite 403C, Atlanta, GA 30322, USA.

Current Hypertension Reports
|March 28, 2008
PubMed
Summary

Reduced tetrahydrobiopterin (BH(4)) availability impairs nitric oxide (NO) production, leading to endothelial dysfunction. BH(4) supplementation may treat conditions like hypertension and diabetes.

Area of Science:

  • Vascular Physiology
  • Endothelial Function
  • Biochemistry

Background:

  • The endothelium is crucial for vascular health, primarily via nitric oxide (NO) signaling.
  • Endothelial dysfunction, linked to reduced NO availability, underlies various cardiovascular diseases.
  • The precise biochemical pathways causing diminished NO production remain incompletely understood.

Purpose of the Study:

  • To investigate the role of tetrahydrobiopterin (BH(4)) in endothelial NO production.
  • To explore BH(4) deficiency as a key factor in endothelial dysfunction.
  • To evaluate BH(4) supplementation as a therapeutic strategy for endothelial dysfunction.

Main Methods:

  • Review of preclinical and clinical studies on BH(4) and endothelial function.

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  • Analysis of factors contributing to reduced BH(4) availability.
  • Assessment of emerging BH(4) drug formulations.

    • Main Results:

    • Reduced BH(4) availability is strongly implicated in decreased NO production.
    • BH(4) deficiency plays a central role in endothelial dysfunction across various conditions.
    • BH(4) supplementation shows promise for treating endothelial dysfunction.

    Conclusions:

    • Tetrahydrobiopterin (BH(4)) is essential for endothelial nitric oxide synthase (eNOS) activity.
    • Restoring BH(4) levels may reverse or mitigate endothelial dysfunction.
    • BH(4) represents a potential therapeutic target for cardiovascular risk and disease states.