hemoprotein การใช้

• These molecules are an important component of the hemoproteins, such as hemoglobin, myoglobin and various cytochromes.
• Hemoproteins achieve their remarkable functional diversity by modifying the environment of the heme macrocycle within the protein matrix.
• Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
• A "'cytochrome "'is a hemoprotein whose main function is electron or proton transfer.
• It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and seal brain.
• The hemoprotein is then detached from the mitochondrial inner membrane and can be extruded into the soluble cytoplasm through pores in the outer membrane.
• The enzymes from the nitrifying bacterium " Nitrosomonas europaea " and the methylotrophic bacterium " Methylococcus capsulatus " are hemoproteins.
• Some examples of conjugated proteins are lipoproteins, glycoproteins, phosphoproteins, hemoproteins, flavoproteins, metalloproteins, phytochromes, cytochromes, opsins and chromoproteins.
• Like all members of this family, it is a hemoprotein, i . e . a protein containing a heme group with an iron atom.
• Some heme-containing enzymes, such as P450s and hemoprotein nitrite reductase, are often named " cytochromes " as well, even though their main function is catalysis.
• Nitroindazole acts as a selective inhibitor for neuronal nitric oxide synthase, a hemoprotein enzyme that, in neuronal tissue, converts arginine to citrulline and nitric oxide ( NO ).
• "' Cytochromes " b " 5 "'are ubiquitous electron transport hemoproteins found in animals, plants, fungi and animal tissues are water-soluble.
• It has been speculated that the original evolutionary function of hemoproteins was electron transfer in primitive sulfur-based photosynthesis pathways in ancestral cyanobacteria-like organisms before the appearance of molecular oxygen.
• NOSs are hemoproteins that combine reductase and oxygenase catalytic domains in one monomer to synthesize NO from the terminal nitrogen atom of L-arginine in the presence of NADPH and O 2.
• Lignin peroxidase ( also " ligninase ", EC number 1.14.99 ) is a hemoprotein firstly isolated from the white-rot fungus " Phanerochaete chrysosporium " with a variety of lignin-degrading reactions, all utilizing hydrogen peroxide as an oxygen source.
• NOSs can be dimeric, calmodulin-dependent or calmodulin-containing cytochrome p450-like hemoprotein that combines reductase and oxygenase catalytic domains in one dimer, bear both flavin adenine dinucleotide ( FAD ) and flavin mononucleotide ( FMN ), and carry out a 5 `-electron oxidation of non-aromatic amino acid arginine with the aid of tetrahydrobiopterin.
• "' Cytochrome P450 reductase "'(; also known as NADPH : ferrihemoprotein oxidoreductase, NADPH : hemoprotein oxidoreductase, NADPH : P450 oxidoreductase, P450 reductase, "'POR "', CPR, CYPOR ) is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 in the endoplasmic reticulum of the cell.
• The family of cytochrome " b " 5-like proteins includes ( besides cytochrome " b " 5 itself ) hemoprotein domains covalently associated with other redox domains in flavocytochrome cytochrome " b " 2 ( L-lactate dehydrogenase; ), sulfite oxidase ( ), plant and fungal nitrate reductases (,, ), and plant and fungal cytochrome " b " 5 / acyl lipid desaturase fusion proteins.