Примеры использования Heme на Английском языке и их переводы на Русский язык
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Heme bp then transfers the electron to heme bn.
Two histidine residues from each subunit coordinate the heme.
Effect of the metal-ligand interaction in the heme group on the colour of myoglobin forms.
The primary reason is the high bioavail- ability of heme iron.
This very complicated protein contains heme A at two different sites, each with a different function.
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Stigmatellin binds farther from heme bL and nearer the Rieske Iron sulfur protein, with which it strongly interacts.
Current practice is tending to measure and report the molar ratio of ZPP to heme μmole/mole.
Heme is exposed to enzymes and is converted into indirect bilirubin, which is fat-soluble toxic substance.
Stercobilin is a tetrapyrrolic bile pigment andis one end-product of heme catabolism.
Bilirubin is formed from the heme portion of hemoglobin released by aged or damaged red blood cells.
Problem 2 Myoglobin for Oxygen Storage Myoglobin(Mb)is a protein containing a heme(iron) group.
For example, ferrochelatase converts the compound into heme b i.e. Fe-protoporphyrin IX or protoheme IX.
A cytochrome is a kind of electron-transferring protein that contains at least one heme group.
TEST PRINCIPLE Bilirubin is formed from the heme portion of hemoglobin released by aged or damaged red blood cells.
Protoporphyrin IX is an important precursor to biologically essential prosthetic groups such as heme, cytochrome c, and chlorophylls.
Heme O, found in the bacterium Escherichia coli, functions in a similar manner to heme A in mammalian oxygen reduction.
Cofactors can be either inorganic(e.g., metal ions and iron-sulfur clusters) or organic compounds e.g.,flavin and heme.
The second electron is transferred to heme bL which then transfers it to heme bH which then transfers it to PQ.
Transition metal ions are optically active in the visible region, which are represented by iron ions,as a part of heme of myoglobin.
Macrophages break down senescent erythrocytes and break the heme down into biliverdin, which normally rapidly reduces to free bilirubin.
It has also been proposed that a gating mechanism may be in place to prevent the electrons from tunneling directly to the heme from the cluster.
Iron ion in the myoglobin heme group of one of the six coordinate bonds can interact with ligands which have various polarizabilities.
Zinc protoporphyrin(ZPP) is a compound found in red blood cells when heme production is inhibited by lead and/or by lack of iron.
Myeloperoxidase contains a heme pigment, which accounts for the green color of secretions rich in neutrophils, such as pus and infected sputum.
The colour shift in case of transformation of one myoglobin form to another is regarded in terms of metal-ligand interaction in the pigment heme group.
The set of processes initiated by oxidation of the iron ion of the heme group is accompanied by generation of reactive oxygen species and hydroxyl ions.
Like heme B, heme A is often attached to the apoprotein through a coordinate bond between the heme iron and a conserved amino acid side-chain.
Antimycin A binds tothe Qi site and inhibits the transfer of electrons in Complex III from heme bH to oxidized Q Qi site inhibitor.
Perhaps because of the two covalent bonds holding the heme to the protein, the iron of heme C is sometimes axially ligated to the amino group of lysine or even water.