Aconitases are iron-sulfur proteins that require a 4Fe-4S cluster for their enzymatic activity, in which they catalyze conversion of citrate to isocitrate.

This protein was harvested from the species Oryctolagus cuniculus, more commonly known as a rabbit.

This protein has a couple of conformational changes associated with it to explain the alternative functions as either mRNA regulator or as an enzyme.

This information was obtained from the RCSB protein data bank website.

Since iron is tightly bound to transferrin, cells throughout the body have receptors for transferrin-iron complexes on their surfaces.

In human cells, the best-characterized iron-sensing mechanism is the result of post-transcriptional regulation of mRNA (the chemical instructions derived from DNA genes to make proteins).

Iron-responsive element-binding protein (IRE-BP) binds to these mRNA sequences.

But, as iron binds to more and more IRE-BPs, they change shape and unbind the transferrin receptor mRNA.