Signaling by H2S is proposed to occur via persulfidation, a posttranslational modification of
cysteine residues (RSH) to persulfides (RSSH). Persulfidation provides a framework for …

Abstract Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are
involved in numerous cellular processes such as respiration, photosynthesis, metabolic …

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 …

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

Abstract Iron–sulphur (Fe–S) clusters have long been recognized as essential and versatile
cofactors of proteins involved in catalysis, electron transport and sensing of ambient …

Mitochondria play a key role in iron metabolism in that they synthesize heme, assemble iron–
sulfur (Fe/S) proteins, and participate in cellular iron regulation. Here, we review the latter …

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 …

Hydrogenases (H2ases) catalyze the reversible oxidation of molecular hydrogen and play a
central role in microbial energy metabolism. Most of these enzymes are found in Archaea …

The iron-molybdenum cofactor (FeMo-co), located at the active site of the molybdenum
nitrogenase, is one of the most complex metal cofactors known to date. During the past …