Related Experiment Video
Updated: Jul 24, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Biosynthesis of iron-sulphur clusters is a complex and highly conserved process
J Frazzon1, J R Fick, D R Dean
1Department of Food Sciences, ICTA, Federal University of Rio Grande do Sul, Porto Allegre, RS, 91051-970, Brazil.
Abstract:
Iron-sulphur ([Fe-S]) clusters are simple inorganic prosthetic groups that are contained in a variety of proteins having functions related to electron transfer, gene regulation, environmental sensing and substrate activation. In spite of their simple structures, biological [Fe-S] clusters are not formed spontaneously. Rather, a consortium of highly conserved proteins is required for both the formation of [Fe-S] clusters and their insertion into various protein partners. Among the [Fe-S] cluster biosynthetic proteins are included a pyridoxal phosphate-dependent enzyme (NifS) that is involved in the activation of sulphur from l-cysteine, and a molecular scaffold protein (NifU) upon which [Fe-S] cluster precursors are formed. The formation or transfer of [Fe-S] clusters appears to require an electron-transfer step. Another complexity is that molecular chaperones homologous to DnaJ and DnaK are involved in some aspect of the maturation of [Fe-S]-cluster-containing proteins. It appears that the basic biochemical features of [Fe-S] cluster formation are strongly conserved in Nature, since organisms from all three life Kingdoms contain the same consortium of homologous proteins required for [Fe-S] cluster formation that were discovered in the eubacteria.
Related Concept Videos
Electron Transport Chains
The ETC is comprised of...
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
The Supercomplexes in the Crista Membrane
Sulfur Assimilation
Microbes and the Sulfur Cycle
Microbes and Other Elemental Cycles

