作者: Chunmei Lu , Gang Xie , Mengyao Liu , Hui Zhu , Benfang Lei
DOI: 10.1371/JOURNAL.PONE.0037556
关键词:
摘要: The heme acquisition machinery in Group A Streptococcus (GAS) consists of the surface proteins Shr and Shp ATP-binding cassette transporter HtsABC. cannot directly acquire from methemoglobin (metHb) but transfers its to HtsA. It has not been previously determined whether relays metHb Shp. Thus, complete pathway for by GAS remained unclear. In this study, metHb-to-Shr Shr-to-Shp transfer reactions were characterized spectroscopy, kinetics protein-protein interaction analyses. Heme is efficiently transferred β α subunits with rates that are 7 60 times greater than those passive release metHb, indicating acquires metHb. rapid involves an initial donor/acceptor complex a spectrally kinetically detectable intermediate, implying channeled present results show speeds up Shp, whereas Furthermore, findings demonstrate can interact Taken together our published on Shp/HtsA reaction, these establish model which extracts it