ArticleBiochemistry2015
Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- The Exoproteome and Surfaceome of ToxigenicJournal of proteome research · 2025Article
- Interactions of azole-based inhibitors with human heme oxygenase.Journal of inorganic biochemistry · 2023Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- Whole genome sequence of a non-toxigenic Corynebacterium diphtheriae strain from a hospital in southeastern China.BMC genomic data · 2021Article
- An Integrated Database of Small RNAs and Their Interplay With Transcriptional Gene Regulatory Networks in Corynebacteria.Frontiers in microbiology · 2021Article
- Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.The FEBS journal · 2020Article
- Active Sites of OBiochemistry · 2017Article
- Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Journal of inorganic biochemistry · 2017Article
- Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016Review
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Authors and funding
10 authors.
Funding
Abstract
The heme uptake pathway (hmu) of Corynebacterium diphtheriae utilizes multiple proteins to bind and transport heme into the cell. One of these proteins, HmuT, delivers heme to the ABC transporter HmuUV. In this study, the axial ligation of the heme in ferric HmuT is probed by examination of wild-type (WT) HmuT and a series of conserved heme pocket residue mutants, H136A, Y235A, and M292A. Characterization by UV-visible, resonance Raman, and magnetic circular dichroism spectroscopies indicates that H136 and Y235 are the axial ligands in ferric HmuT. Consistent with this assignment of axial ligands, ferric WT and H136A HmuT are difficult to reduce while Y235A is reduced readily in the presence of dithionite. The FeCO Raman shifts in WT, H136A, and Y235A HmuT-CO complexes provide further evidence of the axial ligand assignments. Additionally, these frequencies provide insight into the nonbonding environment of the heme pocket. Ferrous Y235A and the Y235A-CO complex reveal that the imidazole of H136 exists in two forms, one neutral and one with imidazolate character, consistent with a hydrogen bond acceptor on the H136 side of the heme. The ferric fluoride complex of Y235A reveals the presence of at least one hydrogen bond donor on the Y235 side of the heme. Hemoglobin utilization assays showed that the axial Y235 ligand is required for heme uptake in HmuT.
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