ArticleBMC structural biology2011
Structural analysis of heme proteins: implications for design and prediction.
Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed, 158 citations in OpenAlex.
- RCSB protein data Bank: Next-generation advanced search for exploration of experimental structures and computed structure models.Protein science : a publication of the Protein Society · 2026Article
- Analysis of putative heme ligands in the System I bacterial cytochromeMicrobiology spectrum · 2026Article
- Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026Article
- A reversible feedback mechanism regulating mitochondrial heme synthesis.The Journal of biological chemistry · 2026Article
- Zinc Sulfate Alleviates Olanzapine Induced Alteration in Hepatic Protein Patterns and Antioxidant Defense System in Rats.Biological trace element research · 2026Article
- Cutibacterium Adaptation to Life on Humans Provides a Potential C acnes Infection Biomarker.The Journal of investigative dermatology · 2026Article
- Label-free photoacoustic imaging of glassfrog development.Photoacoustics · 2025Article
- Comparative Dynamics Enables Discovery of Embedded Bacterial Ferredoxin Domains in Large Redox Enzymes.Proteins · 2025Article
- A reversible feedback mechanism regulating mitochondrial heme synthesis.bioRxiv : the preprint server for biology · 2025Article
- Learning Universal Representations of Intermolecular Interactions with ATOMICA.bioRxiv : the preprint server for biology · 2025Article
- Evolutionary-conserved RLF, a cytochrome bThe New phytologist · 2025Article
- A Novel Spectral Barcoding and Classification Approach for Complex Biological Samples Using Multiexcitation Raman Spectroscopy (MX-Raman).Analytical chemistry · 2025Article
- Article
- Cytochromes P460 and c'-β: exploiting a novel fold for multiple functions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Flexible iron: disorder in the ironome brings order to protein structure and function.Frontiers in molecular biosciences · 2025Article
- The Neural Palette of Heme: Altered Heme Homeostasis Underlies Defective Neurotransmission, Increased Oxidative Stress, and Disease Pathogenesis.Antioxidants (Basel, Switzerland) · 2024Review
- Exploring structural diversity across the protein universe with The Encyclopedia of Domains.Science (New York, N.Y.) · 2024Article
- Heme o Isolation and Analysis Using Heme o Synthase Heterologously Expressed in Escherichia coli.Methods in molecular biology (Clifton, N.J.) · 2024Article
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- Oxidized hemoglobin triggers polyreactivity and autoreactivity of human IgG via transfer of heme.Communications biology · 2023Article
27 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundHeme is an essential molecule and plays vital roles in many biological processes. The structural determination of a large number of heme proteins has made it possible to study the detailed chemical and structural properties of heme binding environment. Knowledge of these characteristics can provide valuable guidelines in the design of novel heme proteins and help us predict unknown heme binding proteins.
resultsIn this paper, we constructed a non-redundant dataset of 125 heme-binding protein chains and found that these heme proteins encompass at least 31 different structural folds with all-α class as the dominating scaffold. Heme binding pockets are enriched in aromatic and non-polar amino acids with fewer charged residues. The differences between apo and holo forms of heme proteins in terms of the structure and the binding pockets have been investigated. In most cases the proteins undergo small conformational changes upon heme binding. We also examined the CP (cysteine-proline) heme regulatory motifs and demonstrated that the conserved dipeptide has structural implications in protein-heme interactions.
conclusionsOur analysis revealed that heme binding pockets show special features and that most of the heme proteins undergo small conformational changes after heme binding, suggesting the apo structures can be used for structure-based heme protein prediction and as scaffolds for future heme protein design.
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Registered trials
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.