ArticleJournal of inorganic biochemistry2017
Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.
Article in Journal of inorganic biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Development and atomic structure of a new fluorescence-based sensor to probe heme transfer in bacterial pathogens.Journal of inorganic biochemistry · 2023Article
- Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance.Heliyon · 2023Review
- Production of copropophyrin III, biliverdin and bilirubin by the rufomycin producer,Frontiers in microbiology · 2023Article
- The Corynebacterium diphtheriae HbpA Hemoglobin-Binding Protein Contains a Domain That Is Critical for Hemoprotein Binding, Cellular Localization, and Function.Journal of bacteriology · 2021Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
HtaA is a heme-binding protein that is part of the heme uptake system in Corynebacterium diphtheriae. HtaA contains two conserved regions (CR1 and CR2). It has been previously reported that both domains can bind heme; the CR2 domain binds hemoglobin more strongly than the CR1 domain. In this study, we report the biophysical characteristics of HtaA-CR2. UV-visible spectroscopy and resonance Raman experiments are consistent with this domain containing a single heme that is bound to the protein through an axial tyrosine ligand. Mutants of conserved tyrosine and histidine residues (Y361, H412, and Y490) have been studied. These mutants are isolated with very little heme (≤5%) in comparison to the wild-type protein (~20%). Reconstitution after removal of the heme with butanone gave an alternative form of the protein. The HtaA-CR2 fold is very stable; it was necessary to perform thermal denaturation experiments in the presence of guanidinium hydrochloride. HtaA-CR2 unfolds extremely slowly; even in 6.8M GdnHCl at 37°C, the half-life was 5h. In contrast, the apo forms of WT HtaA-CR2 and the aforementioned mutants unfolded at much lower concentrations of GdnHCl, indicating the role of heme in stabilizing the structure and implying that heme transfer is effected only to a partner protein in vivo.
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