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Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme
Sarah M Spigelmyer1, Patricia C Dos Santos1
1Department of Chemistry, Wake Forest University Winston-Salem NC 27106 USA dossanpc@wfu.edu.
RSC Chemical Biology
|April 13, 2026
Summary
Iron-sulfur (Fe-S) clusters are vital for life, with complex biosynthesis pathways. Alternate schemes using sulfide, bypassing cysteine desulfurases, offer new evolutionary strategies for Fe-S cluster formation.
Area of Science:
- Biochemistry
- Molecular Biology
- Astrobiology
Background:
- Iron-sulfur (Fe-S) clusters are essential cofactors found in all life domains.
- Fe-S proteins are involved in critical biological processes due to their versatile chemistry.
- Complex machinery has evolved for Fe-S cluster biosynthesis and protein targeting.
Purpose of the Study:
- To review the diverse prokaryotic iron-sulfur cluster biogenesis systems.
- To highlight the role of cysteine desulfurases in sulfur mobilization.
- To discuss alternative Fe-S cluster biosynthesis pathways.
Main Methods:
- Literature review of Fe-S cluster biosynthesis.
- Analysis of known Fe-S cluster biogenesis systems (ISC, NIF, SUF, MIS, SMS).
- Examination of sulfur transfer mechanisms and enzyme interactions.
Main Results:
- Five distinct Fe-S cluster biogenesis systems exist in prokaryotes.
- Cysteine desulfurases are key enzymes utilizing cysteine as a sulfur source.
- Alternative pathways using sulfide bypass sulfurtransferases, indicating evolutionary flexibility.
Conclusions:
- Fe-S cluster biosynthesis is complex and highly conserved.
- Evolution has provided multiple strategies for Fe-S cluster formation.
- Understanding these pathways is crucial for comprehending life's fundamental biochemistry.
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