Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the
biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and …

Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity.
The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component. The …

Vitamin B 12, cobalamin, is a cobalt-containing ring-contracted modified tetrapyrrole that
represents one of the most complex small molecules made by nature. In prokaryotes it is …

If the atmosphere of the early Earth was hydrogen-rich, 1 it is reasonable to think that
hydrogenases, the enzymes enabling cells to use molecular hydrogen, were probably …

▪ Abstract Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic
groups that are required to sustain fundamental life processes. Owing to their remarkable …

Iron/sulfur centers are key cofactors of proteins intervening in multiple conserved cellular
processes, such as gene expression, DNA repair, RNA modification, central metabolism and …

The broad range of cellular activities carried out by Fe–S proteins means that they have a
central role in the life of most organisms. At the interface between biology and chemistry …

The suf and isc operons of Escherichia coli have been implicated in Fe–S cluster assembly.
However, it has been unclear why E. coli has two systems for Fe–S cluster biosynthesis. We …

The assembly of iron-sulfur (Fe-S) clusters is mediated by complex machinery. In several
proteobacteria, this process involves ISC (Fe-S cluster assembly) machinery composed of at …

SUMMARY Iron-sulfur (Fe-S) clusters are required for critical biochemical pathways,
including respiration, photosynthesis, and nitrogen fixation. Assembly of these iron cofactors …