Heme is an iron-containing complex involved in fundamental cellular functions including oxygen transport. Free heme accumulation blood, during intravascular hemolysis and other pathological conditions, triggers vascular dysfunction, pro-inflammatory, prothrombotic cascade. Studies by May et al present a novel finding that ligand for RAGE binds to the V domain of induces oligomerization. Further...

Iron is an essential nutrient for most living organisms. To acquire iron from their environment, Gram-negative bacteria use TonB-dependent transporters that bind host proteins at the bacterial surface and transport iron or heme to the periplasm via the Ton machinery. TonB-dependent transporters are barrel-shaped outer membrane proteins with 22 transmembrane domains, 11 surface-exposed loops, an...

The bacterial respiratory nitric-oxide reductase (NOR) catalyzes the respiratory detoxification of nitric oxide in bacteria and Archaea. It is a member of the well known super-family of heme-copper oxidases but has a [heme Fe-non-heme Fe] active site rather than the [heme Fe-Cu(B)] active site normally associated with oxygen reduction. Paracoccus denitrificans NOR is spectrally characterized by...

In this paper we present probable structures for derivatives of horseradish and cytochrome c peroxidases and also propose a simple scheme which encompasses the molecular structures and electronic configurations of the derivatives of these and other protoheme proteins in the oxidation states from II to VI. Four lines of evidence are used to define the structures of the heme groups and their asso...

We have constructed defined deletions in the hmuO gene from Corynebacterium diphtheriae and Corynebacterium ulcerans and show that the C. ulcerans hmuO mutation results in a significant reduction in hemoglobin-iron utilization, whereas in C. diphtheriae strains, deletion of hmuO caused no or only partial reduction in the utilization of heme as an iron source. We also show that expression from t...

Hemoglobin is composed of two pairs of globin chains to which are attached four iron-containing metalloporphyrins. Factors regulating hemoglobin synthesis include the availability of iron and the presence of heme. Heme production occurs by enzymatic synthesis and includes a step mediated by aminolevulinic acid dehydrase, which is zinc-dependent and, thus, susceptible to the toxic effects of oth...

The metal iron is a limiting nutrient for bacteria during infection. Bacillus anthracis, the causative agent of anthrax and a potential weapon of bioterrorism, grows rapidly in mammalian hosts, which suggests that it efficiently attains iron during infection. Recent studies have uncovered both heme (isd) and siderophore-mediated (asb) iron transport pathways in this pathogen. Whereas deletion o...

Fe-salicylaldehyde isonicotinoylhydrazone (SIH), which can donate iron to reticulocytes without transferrin as a mediator, has been utilized to test the hypothesis that the rate of iron uptake from transferrin limits the rate of heme synthesis in erythroid cells. Reticulocytes take up 59Fe from [59Fe]SIH and incorporate it into heme to a much greater extent than from saturating concentrations o...

BACKGROUND Excess iron has been shown to induce diabetes in animal models. However, the results from human epidemiologic studies linking body iron stores and iron intake to the risk of type 2 diabetes mellitus (T2DM) are conflicting. In this study, we aimed to systematically evaluate the available evidence for associations between iron intake, body iron stores, and the risk of T2DM. METHODS A...

Non-heme iron enzymes catalyze a wide range of O(2) reactions, paralleling those of heme systems. Non-heme iron active sites are, however, much more difficult to study because they do not exhibit the intense spectral features characteristic of the porphyrin ligand. A spectroscopic methodology was developed that provides significant mechanistic insight into the reactivity of non-heme ferrous act...