Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

There have been significant advances in our understanding of mononuclear nonheme iron
oxygenases since our 1996 Chemical Reviews article, 1 promoted in large part by the many …

In recent years, significant progress has been made in understanding the geometric and
electronic structures of the active sites of non-heme iron enzymes and the contributions of …

Iron− sulfur cluster biosynthesis in both prokaryotic and eukaryotic cells is known to be
mediated by two highly conserved proteins, termed IscS and IscU in prokaryotes. The …

The authors describe basic theoretical concepts of vibrational spectroscopy, address
instrumental aspects and experimental procedures, and discuss experimental and …

The transcription of iron uptake and storage genes in Saccharomyces cerevisiae is primarily
regulated by the transcription factor Aft1. Nucleocytoplasmic shuttling of Aft1 is dependent …

Mononuclear non-heme iron active sites are present in a variety of enzymes involed in a
wide range of important biological functions requiring dioxygen. These include superoxide …

When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site)
exists as a dimeric iron–sulfur-containing holoprotein or as a monomeric apoprotein in …

The type and properties of the Fe− S cluster in recombinant Escherichia coli biotin synthase
have been investigated in as-prepared and dithionite-reduced samples using the …

Quinol oxidation by the bc 1 complex of Rhodobacter sphaeroides occurs from an enzyme–
substrate complex formed between quinol bound at the Qo site and the iron–sulfur protein …