Biochemists have figured out how a complex molecule moves iron around the body

(ORDO NEWS) — The new study provides new insights into how an important class of molecules are created and moved in human cells.

For years, scientists have known that mitochondria, specialized structures within body cells that are essential for respiration and energy production, are involved in the assembly and movement of iron and sulfur cofactors, some of the most important compounds in the human body. But until now, researchers have not understood exactly how this process occurs.

A new study published in the journal Nature Communications shows that these cofactors are transported by a substance called glutathione, an antioxidant that helps prevent some types of cell damage by transporting these important iron cofactors across the membrane barrier.

“Glutathione is especially beneficial because it helps regulate metals such as iron, which are used by red blood cells to make hemoglobin, a protein needed to carry oxygen around the body.

Iron compounds are critical to the proper functioning of cellular biochemistry, and their assembly and transport is a complex process.

We have identified how a specific class of iron cofactors move from one cellular compartment to another through a complex molecular mechanism, allowing them to be used in multiple steps in cellular chemistry,” says James Cowan, co-author of the study and Distinguished Professor of Chemistry and Biochemistry at The Ohio State University.

Iron-sulphur clusters are an important class of compounds that carry out various metabolic processes, such as helping to carry electrons for energy production and the production of key metabolites in the cell, as well as helping to replicate our genetic information.

“But when these clusters don’t work properly, or when key proteins can’t get them, then bad things happen,” Cowan emphasizes.

If the damaged protein cannot function, it can cause a number of diseases, including rare forms of anemia, Friedreich’s ataxia (a disease that causes progressive damage to the nervous system), and a host of other metabolic and neurological disorders.

To study how this important mechanism works, the researchers started with the fungus C. thermophilum, identified a key protein molecule of interest, and produced large amounts of this protein to determine its structure.

The study notes that the protein they studied in C. thermophilum is essentially a cellular twin of the human ABCB7 protein that transports iron-sulfur clusters in humans, making it an ideal model for studying the export of iron-sulfur clusters in humans.

Using a combination of cryoelectron microscopy and computer modeling, the team was able to create a series of structural models detailing the pathway that mitochondria use to export iron cofactors to various locations in the body.

While the findings are vital to understanding the basic building blocks of cellular biochemistry, Cowen said he is excited to see how their discovery could advance medicine and therapy


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