To fulfill their nutritional requirement for iron, bacteria utilize various iron sources which
include the host proteins transferrin and lactoferrin, heme, and low molecular weight iron …

Type 1 secretion systems (T1SS) are wide-spread among Gram-negative bacteria. An
important example is the secretion of the hemolytic toxin HlyA from uropathogenic strains …

Pseudomonas aeruginosa PAO1 encodes two outer membrane receptors, PhuR
(Pseudomonas heme uptake) and HasR (heme assimilation system). The HasR and PhuR …

Haem is the major iron source for bacteria that develop in higher organisms. In these hosts,
bacteria have to cope with nutritional immunity imposed by the host, since haem and iron …

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

Recent progress in genetics, fed by the burst in genome sequence data, has led to the
identification of a host of novel bacterial heme proteins that are now being characterized in …

The extreme limitation of free iron has driven various pathogens to acquire iron from the host
in the form of heme. Specifically, several Gram-negative pathogens secrete a heme binding …

Elucidation of the energetic principles of binding affinity and specificity is a central task in
many branches of current sciences: biology, medicine, pharmacology, chemistry, material …

Domain swapping creates protein oligomers by exchange of structural units between
identical monomers. At present, no unifying molecular mechanism of domain swapping has …

All but a few bacterial species have an absolute need for heme, and most are able to
synthesize it via a pathway that is highly conserved among all life domains. Because heme …