Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor

• Published in: Biochimica et biophysica acta Vol. 1840; no. 10; pp. 3058 - 3066
• Main Authors: Mokry, David Z., Nadia-Albete, Angela, Johnson, Michael K., Lukat-Rodgers, Gudrun S., Rodgers, Kenton R., Lanzilotta, William N.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2014
• Subjects: absorption; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; binding sites; Biological Transport, Active - physiology; circular dichroism spectroscopy; electron paramagnetic resonance spectroscopy; heme; Heme - chemistry; Heme - genetics; Heme - metabolism; heme iron; Heme transport; hemoglobin; Hemoglobin receptor; HmbR; Iron - chemistry; ligands; mammals; microorganisms; Neisseria meningitidis; Neisseria meningitidis - chemistry; Neisseria meningitidis - genetics; Neisseria meningitidis - metabolism; Pathogenesis; pathogens; Protein Binding - physiology; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Receptors, Cell Surface - metabolism; Septic shock; sodium hydrosulfite; spectral analysis; Spectrum Analysis; Ton-B dependent transport; tyrosine; Septic shock; Pathogenesis; HmbR; Heme transport; Hemoglobin receptor; Ton-B dependent transport

For many pathogenic microorganisms, iron acquisition represents a significant stress during the colonization of a mammalian host. Heme is the single most abundant source of soluble iron in this environment. While the importance of iron assimilation for nearly all organisms is clear, the mechanisms b...