「Heme」の共起表現(1語左で並び替え) - Weblio英語共起表現検索

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共起表現

「Heme」の共起表現一覧(1語左で並び替え)

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ecifically those acting on NADH or NADPH with a	heme protein as acceptor.
subunit (PsbE), one beta (PsbF) subunit, and a	heme cofactor.
For instance Cytochrome a has a	heme a prosthetic group and cytochrome b has a heme
iron atom in most cytochromes is contained in a	heme group.
me that utilizes a molybdopterin cofactor and a	heme group.
eme is synthesized from uroporphyrinogen III, a	heme and vitamin B12 precursor.
Transport vesicle delivering a	heme detoxification protein (hdp) to a malaria food
oxidoreductases, specifically those acting on a	heme group of donors with other acceptors.
They each contain a	heme prosthetic group covalently bound by two ester
hole” in the special pair by an electron from a	heme in cytochrome c.
uorin is that chlorocruorin carries an abnormal	heme group structure.
chetalase enzyme is the last step before actual	heme production and then actual hemoglobin productio
utosomal recessive metabolic disorder affecting	heme, caused by deficiency of the enzyme uroporphyri
It has 2 cofactors: FAD, and	Heme.
It has 3 cofactors: NADH, NADPH, and	Heme.
e 3 substrates of this enzyme are ATP, H2O, and	heme, whereas its 3 products are ADP, phosphate, and
chrome c, and two products, apocytochrome c and	heme.
For example, flavin and	heme cofactors are often involved in redox reactions
The rate-limiting enzyme in porphyrin and	heme biosynthesis is ALA synthase, the enzyme (EC 2.
Chlorophyll is a magnesium porphyrin, and	heme is an iron porphyrin, but neither porphyrin is
ns that have other prosthetic groups as well as	heme c.
must modify protoporphyrin IX before it becomes	heme.
stingly, all members of the Rev-erb family bind	heme, which may act as a ligand to regulate their tr
Hemopexin binds	heme with the highest affinity of any known protein.
turn hydrogen-bonded to a propionate of the bL	heme.
other electron, which was transferred to the bL	heme, is used to reduce the bH heme, which in turn t
ieske iron-sulfur '(FeS) protein' and to the bL	heme.
The histidine bound	heme group of succinate dehydrogenase, an electron c
h Political Will, in Silence and Mass Murder by	Heme Kake Rash, Sardam Publishing House, April 2008.
n, hemoglobin, or certain cytochromes is called	heme.
It employs one cofactor,	heme.
It has 2 cofactors:	heme, and Molybdenum.
450-production, induced by the drugs, consuming	heme.
uric acid, the other is dark (black) containing	heme.
Hence, the Rev-erbα receptor detects	heme and thereby coordinates the cellular clock, glu
contain nitric oxide (NO) ligated to the ferric	heme iron (Fe3+).
yoglobin, and cytochrone c by oxidizing ferrous	heme into its corresponding ferric forms.
rotoporphyrin IX is combined with iron to form	heme. Bile pigments are the breakdown products of he
ous organisms against the toxic effects of free	heme.
s the transfer of electrons in Complex III from	heme bH to oxidized Q (Qi site inhibitor).
Generally,	heme B is attached to the surrounding protein matrix
HMOX1 (	heme oxygenase (decycling) 1) is a human gene that e
Since the iron in	heme B containing proteins is bound to the four nitr
In	heme biosynthesis, the enzyme ferrochelatase convert
The enzyme complexes vary in	heme and copper composition, substrate type and subs
yme that is responsible for the seventh step in	heme production.
the enzyme responsible for the seventh step in	heme production.
PDB 1URO) which catalyzes the fifth step in	heme biosynthesis: the elimination of carboxyl group
Red blood cells are rich in iron-containing	heme.
o capable of oxidizing these substrates but its	heme is not covalently bound and becomes damaged dur
body, releasing their oxygen-carrying molecule	heme, which is degraded by enzymes into the yellow-g
Its levels in serum reflect how much	heme is present in the blood.
linogen synthase), which is required for normal	heme synthesis.
product of the sixth step in the production of	heme) to form protoporphyrin IX.
ormal physiological conditions, the activity of	heme oxygenase is highest in the spleen, where old e
loroplast structure, and of the biosynthesis of	heme and related molecules.
-conserved cysteine bound to the iron center of	heme B.
volve the compartmentalization and transport of	heme, as well as peptides, from the mitochondria to
hat is one of the natural breakdown products of	heme via choleglobin, verdohemochrome, biliverdin, b
Structure of	Heme B
The correct structure of	heme A, based upon NMR and IR experiments of the red
that there has been significant degradation of	heme containing compounds and hemopexin is made to s
The number of	heme C units bound to a holoprotein is highly variab
erested in elucidating the multifaceted role of	heme in cellular processes.
pyrrolic bile pigment and is one end-product of	heme catabolism.
Its kinase activity is induced by low levels of	heme and inhibited by the presence of heme.
contained within the protoporphyrin IX ring of	heme into proteins.
rface reduction, lowering of pH, utilization of	heme, or extraction of protein-complexed metal.
a half-transporter involved in the transport of	heme from the mitochondria to the cytosol.
When the amount of	heme in the liver decreases, it no longer act as a r
nalogous Corrphycene Derivative: Suppression of	Heme Oxygenase and Reconstitution with Apomyoglobin.
generally agreed the number and arrangement of	heme C groups are related and even required for prop
For vertebrate cells one	heme C per protein is the rule but for bacteria this
ou must shape a sark to me / Without any cut or	heme, quoth he"); she responds with a list of tasks
e difference between aggregated or precipitated	heme, and genuine hemozoin.
Once bound to the prosthetic	heme groups, these molecules can modulate the activi
ication of ahydrophobic cluster in the proximal	heme pocket.
ugh different colors as it gradually heals: red	heme to green biliverdin to yellow bilirubin.
Lysis of these cells releases	heme into the surroundings, allowing the bacteria to
lectron-transfer proteins having one or several	heme c groups, bound to the protein by one or, more
However it has been shown	heme suppresses hepatic gluconeogenic gene expressio
The iron of the	heme A of cytochrome a3 is sometimes bound by 5 othe
rous form of iron into protoporphyrin IX in the	heme synthesis pathway.
ut receives some "supporting electron" from the	heme ligand.
The	heme portion of hemoglobin contains peroxidase and w
of carbon dioxide must bind to a region on the	heme monomer which a molecule of oxygen would not ty
d the oxygen carrying ferrous ion (Fe2+) of the	heme group of the hemoglobin molecule is oxidized to
The	heme moiety of intact hemoglobin is chemically conve
HMOX1 and HMOX2 belong to the	heme oxygenase family.
The	heme is positioned between β-sheet and an α-helix, w
Its function of scavenging the	heme released or lost by the turnover of heme protei
tection of diatomic gases, the gas binds to the	heme iron.
This gene encodes the fifth enzyme of the	heme biosynthetic pathway.
Newer findings however, indicate that the	heme moiety is also produced by the plant.
pigment that results from the breakdown of the	heme portion of hemoglobin.
It is common for the	heme C to amino acid ratio to be high for bacterial
The	heme iron serves as a source or sink of electrons du
s between the two cysteinyl groups bound to the	heme.
The iron of the	heme A of cytochrome a is hexacoordinated, that is b
break down senescent erythrocytes and break the	heme down into biliverdin, which rapidly reduces to
mic gases, the binding of the gas ligand to the	heme iron induces conformational changes in the surr
A third	heme oxygenase (HO-3) is not catalytically active, b
This	heme has to be drawn then as radical cation (.+).
Interestingly, NO can bind both to	heme Fe3+ and to proximal Cys-60 ligand causing reve
The two thioether bonds are made to	heme ring positions 2 and 4, but a few c type cytoch
on transfer from the cytosol to a transmembrane	heme moiety.
responsible for electron transport, binding two	heme groups non-covalently.
another important enzyme that contains a C type	heme.
related substances that are also released when	heme is metabolized are oxyhemoglobin and methemoglo

共起表現