The surface protein Shr of binds heme and transfers it to the streptococcal heme-binding protein Shp-0

20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm were recorded. (A) The normalized spectral changes Δ(A-A) (green curve) and Δ(A-A) (red curve) for the methemoglobin/apoShp and methemoglobin/apomyoglobin reactions, respectively. The black curves are the theoretical curves obtained by fitting the data to a two exponential equation. (B) Δ(A-A) of the methemoglobin/apoShp reaction does not fit a single exponential equation. The dashed and solid curves are respectively the observed data and theoretical curve from fitting of the data to a single exponential equation.<p><b>Copyright information:</b></p><p>Taken from "The surface protein Shr of binds heme and transfers it to the streptococcal heme-binding protein Shp"</p><p>http://www.biomedcentral.com/1471-2180/8/15</p><p>BMC Microbiology 2008;8():15-15.</p><p>Published online 23 Jan 2008</p><p>PMCID:PMC2266757.</p><p>