ArticleProteins2008
Ligand preference and orientation in b- and c-type heme-binding proteins.
Article in Proteins, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 46 citations in OpenAlex.
- Diversity and evolution of nitric oxide reduction in bacteria and archaea.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Depletion assisted hemin affinity (DAsHA) proteomics reveals an expanded landscape of heme-binding proteins in the human proteome.Metallomics : integrated biometal science · 2023Article
- A Chemical Proteomic Map of Heme-Protein Interactions.Journal of the American Chemical Society · 2022Article
- A noncanonical cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The redox potential of a heme cofactor inPhysical chemistry chemical physics : PCCP · 2021Article
- Identifying metal binding amino acids based on backbone geometries as a tool for metalloprotein engineering.Protein science : a publication of the Protein Society · 2021Article
- Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins.ACS nano · 2021Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- The pigment binding behaviour of water-soluble chlorophyll protein (WSCP).Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020Article
- HeMoQuest: a webserver for qualitative prediction of transient heme binding to protein motifs.BMC bioinformatics · 2020Article
- Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme.Frontiers in bioengineering and biotechnology · 2019Article
- In-Cell Enzymology To Probe His-Heme Ligation in Heme Oxygenase Catalysis.Biochemistry · 2016Article
- Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.Journal of inorganic biochemistry · 2016Article
- Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.The Journal of biological chemistry · 2016Article
- SCMHBP: prediction and analysis of heme binding proteins using propensity scores of dipeptides.BMC bioinformatics · 2014Article
- Redox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552.The journal of physical chemistry. B · 2013Article
- Direct tests of enzymatic heme degradation by the malaria parasite Plasmodium falciparum.The Journal of biological chemistry · 2012Article
- Prediction of heme binding residues from protein sequences with integrative sequence profiles.Proteome science · 2012Article
- Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases.Frontiers in pharmacology · 2012Article
- Modulation of ligand-field parameters by heme ruffling in cytochromes c revealed by EPR spectroscopy.Inorganic chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hemes are often incorporated into designed proteins. The importance of the heme ligand type and its orientation is still a matter of debate. Here, heme ligands and ligand orientation were investigated using a nonredundant (87 structures) and a redundant (1503 structures) set of structures to compare and contrast design features of natural b- and c-type heme-binding proteins. Histidine is the most common ligand. Marked differences in ligation motifs between b- and c-type hemes are higher occurrence of His-Met in c-type heme binding motifs (16.4% vs. 1.4%) and higher occurrence of exchangeable, small molecules in b-type heme binding motifs (67.6% vs. 9.9%). Histidine ligands that are part of the c-type CXXCH heme-binding motif show a distinct asymmetric distribution of orientation. They tend to point between either the heme propionates or between the NA and NB heme nitrogens. Molecular mechanics calculations show that this asymmetry is due to the bonded constraints of the covalent attachment between the heme and the protein. In contrast, the orientations of b-type hemes histidine ligands are found evenly distributed with no preference. Observed histidine heme ligand orientations show no dominating influence of electrostatic interactions between the heme propionates and the ligands. Furthermore, ligands in bis-His hemes are found more frequently perpendicular rather than parallel to each other. These correlations support energetic constraints on ligands that can be used in designing proteins.
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