Function Coupling Mechanism of PhuS and HemO in Heme Degradation
نویسندگان
چکیده
منابع مشابه
Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO).
Iron, an essential nutrient with limited bioavailability, requires specialized cellular mechanisms for uptake. Although iron uptake into the cytoplasm in the form of heme has been well characterized in many bacteria, the subsequent trafficking is poorly understood. The cytoplasmic heme-binding proteins belong to a structurally related family thought to have evolved as "induced fit" ligand-bindi...
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15 صفحه اولLigand-induced allostery in the interaction of the Pseudomonas aeruginosa heme binding protein with heme oxygenase.
A heme-dependent conformational rearrangement of the C-terminal domain of heme binding protein (PhuS) is required for interaction with the iron-regulated heme oxygenase (HemO). Herein, we further investigate the underlying mechanism of this conformational rearrangement and its implications for heme transfer via site-directed mutagenesis, resonance Raman (RR), hydrogen-deuterium exchange MS (HDX...
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Background: Malaria is one of the most important parasitic diseases in the world caused by Plasmodium species. The malaria parasite digests hemoglobin in vacuole to amino acids and heme. Plasmodium has got several detoxification mechanisms to protect itself from toxic heme. The most important mechanism is heme polymerization. Identifying compounds that inhibit heme polymerization is an approach...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2017
ISSN: 2045-2322
DOI: 10.1038/s41598-017-11907-5