Wydział Chemii

Jacek Wojaczyński

Halina Wójtowicz

Marcin Bielecki

Mariusz Olczak

John W. Smalley

Lechosław Latos-Grażyński

Teresa Olczak

2011

Biochemical and Biophysical Research Communications

411

299-304

10.1016/j.bbrc.2011.06.129

Naukowa

Angielski

Artykuł

Porphyromonas gingivalis acquires heme through an outer-membrane heme transporter HmuR and heme-binding hemophore-like lipoprotein HmuY. Here, we compare binding of iron(III) mesoporphyrin IX (mesoheme) and iron(III) deuteroporphyrin IX (deuteroheme) to HmuY with that of iron(III) protoporphyrin IX (protoheme) and protoporphyrin IX (PPIX) using spectroscopic methods. In contrast to PPIX, mesoheme and deuteroheme enter the HmuY heme cavity and are coordinated by His134 and His166 residues in a fully analogous way to protoheme binding. However, in the case of deuteroheme two forms of HmuY–iron porphyrin complex were observed differing by a 180° rotation of porphyrin about the α-γ-meso-carbon axis. Since the use of porphyrins either as active photosensitizers or in combination with antibiotics may have therapeutic value for controlling bacterial growth in vivo, it is important to compare the binding of heme derivatives to HmuY.

Porphyromonas gingivalis, HmuY, Heme-binding protein, Iron, metalloporfyrin

https://doi.org/10.1016/j.bbrc.2011.06.129

http://www.elsevier.com