Mutational analysis of hemoglobin binding and heme utilization by a bacterial hemoglobin receptor.

Mutational analysis of hemoglobin binding and heme utilization by a 4 bacterial hemoglobin receptor

Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization.

The pathogenesis of human infections caused by the gram-positive microbe Staphylococcus aureus has been previously shown to be reliant on the acquisition of iron from host hemoproteins. The iron-regulated surface determinant system (Isd) encodes a heme transport apparatus containing three cell wall-anchored proteins (IsdA, IsdB, and IsdH) that are exposed on the staphylococcal surface and hence...

Heme Releasing from Human Hemoglobin upon Interaction with a New Synthesized Complex of 1,10-Phenanthroline-n-butyl Dithiocarbamato Pd(II) Nitrate

In the present study, we investigated the effect of a new anticancer Pd(II) complex, 1,10-phenanthroline-n-butyl dithiocarbamato Pd(II) nitrate, on the heme releasing from human hemoglobin (Hb) as well as alterations in the structure and function of Hb using different spectroscopic methods of UV-Vis, fluorescence and circular dichroism (CD)at two temperatures of 25 and 37 °C. Fluorescence data ...

Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins, and metalloporphyrins.

Previous genetic and biochemical studies have confirmed that hemoglobin and hemin utilization in Porphyromonas gingivalis is mediated by the outer membrane hemoglobin and heme receptor HmuR, as well as gingipain K (Kgp), a lysine-specific cysteine protease, and gingipain R1 (HRgpA), one of two arginine-specific cysteine proteases. In this study we report on the binding specificity of the recomb...

Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron.

The hemolytic Streptococcus pyogenes can use a variety of heme compounds as an iron source. In this study, we investigate hemoprotein utilization by S. pyogenes. We demonstrate that surface proteins contribute to the binding of hemoproteins to S. pyogenes. We identify an ABC transporter from the iron complex family named sia for streptococcal iron acquisition, which consists of a lipoprotein (s...