heme protein
thumb|420 px|Binding of oxygen to a heme prosthetic group, which would be part of a hemoprotein.
Research
333,877 papers- GalaxyDock2-HEME: Protein-ligand docking for heme proteins.Journal of computational chemistry · 2023
- Heme protein assemblies.Chemical reviews · 2004
- The molecular basis of transient heme-protein interactions: analysis, concept and implementation.Bioscience reports · 2019
- The diversity of heme sensor systems - heme-responsive transcriptional regulation mediated by transient heme protein interactions.FEMS microbiology reviews · 2022
- ACE2 deficiency protects against heme protein-induced acute kidney injury.American journal of physiology. Renal physiology · 2025
via PubMed
Article
11 sectionsContents
- Roles
- Hemoglobin and myoglobin
- Myoglobin
- Hemoglobin
- Neuroglobin
- Peroxidases and catalases
- Electron transport chain and other redox catalysts
- Nitric oxide synthase
- Designed heme proteins
- References
- External links
thumb|420 px|Binding of oxygen to a heme prosthetic group, which would be part of a hemoprotein.
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.