Heme proteins perform various biological functions ranging from electron transfer, oxygen
binding and transport, catalysis, to signaling. Although adopting proper native states is very …

Lanthanide elements have been recently recognized as “new life metals” yet much remains
unknown regarding lanthanide acquisition and homeostasis. In Methylorubrum extorquens …

Cyanobacteria are mainly known to incorporate inorganic molecules like carbon dioxide and
ammonia from the environment into organic material within the cell. Nevertheless …

Proper functioning of the mitochondrion requires the orchestrated assembly of respiratory
complexes with their cofactors. Cytochrome c, an essential electron carrier in mitochondria …

Heme post‐translational modification plays a key role in tuning the structure and function of
heme proteins. We herein report a novel tyrosine–heme covalent C O bond in an artificially …

Heme proteins perform a large array of biological functions using the same heme cofactor. A
primary method of regulating these diverse functions is the heme-protein cross-link, an …

Cytochrome c maturation (ccm) in many bacteria, archaea and plant mitochondria requires
eight membrane proteins, CcmABCDEFGH, called system I. This pathway delivers and …

There is growing evidence for the involvement of Y-complex nucleoporins (Y-Nups) in
cellular processes beyond the inner core of nuclear pores of eukaryotes. To …

The periplasmic heme chaperone holoCcmE is essential for heme trafficking in the
cytochrome c biosynthetic pathway in many bacteria, archaea, and plant mitochondria. This …

Iron-protoporphyrin IX, or b heme, is utilized as such by a large number of proteins and
enzymes. In some cases, notably the c-type cytochromes, this group undergoes a …