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Related to hemoprotein: flavoprotein, heme protein
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.hemoprotein - a conjugated protein linked to a compound of iron and porphyrin
compound protein, conjugated protein - a protein complex combining amino acids with other substances
haemoglobin, Hb, hemoglobin - a hemoprotein composed of globin and heme that gives red blood cells their characteristic color; function primarily to transport oxygen from the lungs to the body tissues; "fish have simpler hemoglobin than mammals"
myoglobin - a hemoprotein that receives oxygen from hemoglobin and stores it in the tissues until needed
cytochrome - (biochemistry) a class of hemoprotein whose principal biological function is electron transfer (especially in cellular respiration)
References in periodicals archive ?
The cytochrome b5-like domains include (in addition to the cytochrome b5) hemoprotein domains covalently associated with other redox domains of proteins, such as acyl lipid desaturase fusion protein.
Thyroid peroxidase (TPO) is a membrane-bound glycosylated hemoprotein that has a key role in the biosynthesis of thyroid hormones by organification.
Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3.
3-1) Steroid hydroxylations and the participation of hemoprotein cytochrome P450.
Catalase is a hemoprotein which catalyzes the reduction of hydrogen peroxides and protects the tissues from highly reactive hydroxyl radicals (Kohner et al.
Myoglobin (Mb), a cytoplasmic hemoprotein of 18 kDa, which is present in skeletal and cardiac muscle [10].
It has been suggested that ritonavir reduces the redox potential of the hemoprotein CYP3A4 and prevents it reduction by its redox partner cytochrome P450 reductase.
Myoglobin (Mb), [3] a 17-kDa single-chain oxygen-carrying hemoprotein, appears in the circulation within a few hours of skeletal or cardiac muscle damage and is rapidly filtered by the glomeruli and reabsorbed by the proximal tubules where it is catabolized (1-3).
Effect of temperature on structural and functional properties of horseradish peroxidases was established that temperatures ranged 20-55oC causes reversible conformation and occurrence of changes of the hemoprotein molecule, which is related to consequent unfolding and folding of the protein globule.
This production of NO is due to NO synthase (NOS), a hemoprotein enzyme that catalyzes the conversion of L-arginine to L-citrulline and NO.
The hemoprotein biocatalyst can be contacted with the fossil fuel in free or immobilized forms.