Related Experiment Video
Updated: May 20, 2026

11:25
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
Published on: March 18, 2017
Interaction between the heme and a G-quartet in a heme-DNA complex
Kaori Saito1, Hulin Tai, Hikaru Hemmi
1Department of Chemistry, University of Tsukuba, Tsukuba 305-8571, Japan.
Inorganic Chemistry
|July 27, 2012
Summary
Researchers used NMR to study heme(Fe(3+)) and G-quadruplex DNA complexes. They found heme(Fe(3+)) binds within the DNA G-quartets, influencing its electronic structure and offering insights for heme-DNA complex design.
Area of Science:
- Biochemistry
- Structural Biology
- Chemical Biology
Background:
- G-quadruplex DNA structures are important in telomere maintenance and gene regulation.
- Heme-DNA complexes have potential applications in diagnostics and therapeutics.
Purpose of the Study:
- To characterize the structure of a complex formed between heme(Fe(3+)) and a human telomere G-quadruplex DNA sequence.
- To elucidate the interaction between heme and G-quadruplex DNA at a molecular level.
Main Methods:
- Proton Nuclear Magnetic Resonance ((1)H NMR) spectroscopy was employed.
- Analysis of solvent (1)H/(2)H isotope effects on NMR parameters.
Main Results:
- The structure revealed heme(Fe(3+)) is sandwiched between the 3'-terminal G-quartets of the d(TTAGGG) G-quadruplex.
- The positively charged heme(Fe(3+)) interacts with eight carbonyl oxygen atoms of the G-quartets.
- This interaction creates a strong, axially symmetric ligand field, resulting in a low-spin heme(Fe(3+)) species with a highly symmetric electronic structure.
Conclusions:
- The study provides detailed structural insights into heme-G-quadruplex DNA complexes.
- Findings advance understanding of heme-DNA interactions and inform the design of novel heme-DNA architectures and functional molecules.
Related Concept Videos
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...
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...
ROS generation is regulated and maintained at moderate levels necessary...
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Activation and Inactivation of G Proteins
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Hemoglobin
Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Globular Proteins
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...

