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

Weblio 辞書 > 英和辞典・和英辞典 > Hemeの意味・解説 > Hemeに関連した共起表現

意味

例文

類語

共起表現

「Heme」の共起表現一覧(1語右で並び替え)

該当件数 : 124件

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

共起表現