ArticleThe Journal of biological chemistry2012
Role of the iron axial ligands of heme carrier HasA in heme uptake and release.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Hemophore-like proteins of the HmuY family in the oral and gut microbiome: unraveling the mystery of their evolution.Microbiology and molecular biology reviews : MMBR · 2024Review
- Axial Heme Coordination by the Tyr-His Motif in the Extracellular Hemophore HasAp Is Critical for the Release of Heme to the HasR Receptor ofBiochemistry · 2021Article
- Contributions of the heme coordinating ligands of theThe Journal of biological chemistry · 2020Article
- Structural insights into heme binding to IL-36α proinflammatory cytokine.Scientific reports · 2019Article
- Post-transcriptional regulation of theThe Journal of biological chemistry · 2019Article
- The molecular basis of transient heme-protein interactions: analysis, concept and implementation.Bioscience reports · 2019Review
- 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
- A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase.Biochemistry · 2016Article
- Article
- Spectroscopic and mutagenesis studies of human PGRMC1.Biochemistry · 2015Article
- A relay network of extracellular heme-binding proteins drives C. albicans iron acquisition from hemoglobin.PLoS pathogens · 2014Article
- Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor.Biochimica et biophysica acta · 2014Article
- NMR investigations of nitrophorin 2 belt side chain effects on heme orientation and seating of native N-terminus NP2 and NP2(D1A).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Replacing the axial ligand tyrosine 75 or its hydrogen bond partner histidine 83 minimally affects hemin acquisition by the hemophore HasAp from Pseudomonas aeruginosa.Biochemistry · 2014Article
- Heme uptake in bacterial pathogens.Current opinion in chemical biology · 2014Review
- The IR-¹⁵N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules.Journal of biomolecular NMR · 2014Article
- Electron spin density on the axial His ligand of high-spin and low-spin nitrophorin 2 probed by heteronuclear NMR spectroscopy.Inorganic chemistry · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
The hemophore protein HasA from Serratia marcescens cycles between two states as follows: the heme-bound holoprotein, which functions as a carrier of the metal cofactor toward the membrane receptor HasR, and the heme-free apoprotein fishing for new porphyrin to be taken up after the heme has been delivered to HasR. Holo- and apo-forms differ for the conformation of the two loops L1 and L2, which provide the axial ligands of the iron through His(32) and Tyr(75), respectively. In the apo-form, loop L1 protrudes toward the solvent far away from loop L2; in the holoprotein, closing of the loops on the heme occurs upon establishment of the two axial coordination bonds. We have established that the two variants obtained via single point mutations of either axial ligand (namely H32A and Y75A) are both in the closed conformation. The presence of the heme and one out of two axial ligands is sufficient to establish a link between L1 and L2, thanks to the presence of coordinating solvent molecules. The latter are stabilized in the iron coordination environment by H-bond interactions with surrounding protein residues. The presence of such a water molecule in both variants is revealed here through a set of different spectroscopic techniques. Previous studies had shown that heme release and uptake processes occur via intermediate states characterized by a Tyr(75)-iron-bound form with open conformation of loop L1. Here, we demonstrate that these states do not naturally occur in the free protein but can only be driven by the interaction with the partner proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.