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Protein containing a heme prosthetic group
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very
Hemoprotein
Chemical coordination complex of an iron ion chelated to a porphyrin
one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the
Heme
Enzyme
enzymology, a NADPH—hemoprotein reductase is an enzyme that catalyzes the chemical reaction NADPH + H+ + n oxidized hemoprotein ⇌ {\displaystyle \rightleftharpoons
NADPH—hemoprotein_reductase
Mammalian protein found in humans
reductase (also known as NADPH:ferrihemoprotein oxidoreductase, NADPH:hemoprotein oxidoreductase, NADPH:P450 oxidoreductase, P450 reductase, POR, CPR,
Cytochrome_P450_reductase
Iron and oxygen-binding protein
close approach of the Fe-porphyrin assemblies. Cytoglobin Hemoglobin Hemoprotein Neuroglobin Phytoglobin Myoglobinuria - The presence of myoglobin in
Myoglobin
Protein that contains a non-peptide component
Transport is one of the most important roles of conjugated proteins. Hemoproteins are a type of conjugate proteins that help facilitate the transportation
Conjugated_protein
Protein-coding gene in the species Homo sapiens
cofactors to catalyse the reaction: NADPH + H+ + n oxidised hemoprotein = NADP+ + n reduced hemoprotein. Binding domain involved in the interaction with proteins
MTRR_(gene)
Type of chemical compound
essential member of the porphyrin group is heme, which is a component of hemoproteins, whose functions include carrying oxygen in the bloodstream. In plants
Porphyrin
Enzyme that metabolizes substances by oxidation
and the most versatile one. Like all members of this family, it is a hemoprotein, i.e. a protein containing a heme group with an iron atom. In humans
CYP3A4
Bloodlike fluid in arthropods
called hemocytes are dispersed in addition to many plasma proteins (hemoproteins) and dissolved chemicals. It is the key component of the open circulatory
Hemolymph
Peroxide-decomposing enzyme
peroxidase Chloride peroxidase Cytochrome c peroxidase Haloperoxidase Hemoprotein Immunoperoxidase Lactoperoxidase Myeloperoxidase (MPO) Thyroid peroxidase
Peroxidase
Protein family
Cytochromes b5 are ubiquitous electron transport hemoproteins found in animals, plants, fungi and purple phototrophic bacteria. The microsomal and mitochondrial
Cytochrome_b5
Metalloprotein that binds with oxygen
Chlorophyll (Mg heme) Complete blood count Delta globin Hemoglobinometer Hemoprotein Methemoglobin (ferric Hb, or ferrihemoglobin) Oxyhemoglobin (with diatomic
Hemoglobin
Mammalian protein found in Homo sapiens
homeostasis and reactive oxygen/nitrogen scavenging. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal
Neuroglobin
Enzyme in neutrophils and other immune cells
Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophils
Myeloperoxidase
Chemical compound
acts as a selective inhibitor for neuronal nitric oxide synthase, a hemoprotein enzyme that, in neuronal tissue, converts arginine to citrulline and
7-Nitroindazole
Poisonous oxygen-carbon compound
which is the catabolic action of heme oxygenase on the heme derived from hemoproteins such as hemoglobin. Following the first report that carbon monoxide is
Carbon_monoxide
Interconnected biochemical reactions releasing energy
intermediate, succinyl-CoA. These molecules are an important component of the hemoproteins, such as hemoglobin, myoglobin and various cytochromes. During gluconeogenesis
Citric_acid_cycle
effect) (3D computer graphics) (demo effects) Bohr effect (hematology) (hemoproteins) (respiratory physiology) Boomerang effect (psychology) (social psychology)
List_of_effects
Medical condition
Within the medical specialty of hematology, Hemoglobin D-Punjab, also known as hemoglobin D-Los Angeles, D-North Carolina, D-Portugal, D-Oak Ridge, and
Hemoglobin_D-Punjab
Class of enzymes
contains 288 amino acid residues encoded by the HMOX1 gene. HO-1 is not a hemoprotein as it does not contain any heme prosthetic groups. The activity of HO-1
Heme_oxygenase
Class of enzymes
calmodulin-dependent or calmodulin-containing cytochrome p450-like hemoprotein that combines reductase and oxygenase catalytic domains in one dimer
Nitric_oxide_synthase
Toxic effects of carbon monoxide
expelling carbon dioxide as carbaminohemoglobin. Additionally, many other hemoproteins such as myoglobin, Cytochrome P450, and mitochondrial cytochrome oxidase
Carbon_monoxide_poisoning
Enzyme decomposing hydrogen peroxide
Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition
Catalase
Chemical compound
compound: zeinoxanthin + reduced [NADPH-hemoprotein reductase] + dioxygen → lutein + oxidized [NADPH-hemoprotein reductase] + H2O Loeber, D. E.; Russell
Zeinoxanthin
Haptoglobin Helicase Hematoxylin Heme Hemerythrin Hemocyanin Hemoglobin Hemoprotein Heparan sulfate High density lipoprotein, HDL Histamine Histidine Histone
List_of_biomolecules
Class of enzymes
steroid + 3 reduced [NADPH–hemoprotein reductase] + 3 O2 = a Delta(14) steroid + formate + 3 oxidized [NADPH–hemoprotein reductase] + 4 H2O + 4 H(+)
Sterol_14-demethylase
Hemoglobin with ferric iron unable to carry oxygen
Methemoglobin (British: methaemoglobin, shortened MetHb) (pronounced "met-hemoglobin") is a hemoglobin in the form of metalloprotein, in which the iron
Methemoglobin
Complex of carbon monoxide and hemoglobin
Hemoglobin variants). Structural variations and mutations across other hemoproteins likewise affect carbon monoxide's interaction with the heme prosthetic
Carboxyhemoglobin
Enzyme
\rightleftharpoons } oxidized donor + 2 H2O Versatile peroxidase is a hemoprotein. Martínez MJ, Ruiz-Dueñas FJ, Guillén F, Martínez AT (April 1996). "Purification
Versatile_peroxidase
Aerobic respiration enzyme
The enzyme cytochrome c oxidase or Complex IV (was EC 1.9.3.1, now reclassified as a translocase EC 7.1.1.9) is a large transmembrane protein complex found
Cytochrome_c_oxidase
Enzyme
converting it to dioxygen (O2) and chloride (Cl−). Chlorite dismutase is a hemoprotein, but it bears no structural or sequence relationships with known peroxidases
Chlorite_dismutase
Protein-coding gene in the species Homo sapiens
a human microsomal cytochrome b5. Cytochrome b5 is a membrane bound hemoprotein which functions as an electron carrier for several membrane bound oxygenases
Cytochrome_b5,_type_A
Chemical compound
(2007-11-27). "Enzymatic synthesis of a bicyclobutane fatty acid by a hemoprotein lipoxygenase fusion protein from the cyanobacterium Anabaena PCC 7120"
Bicyclobutane
Proteins in salvia of bloodfeeding insects
Nitrophorins are hemoproteins found in the saliva of blood-feeding insects. Saliva of the blood-sucking bug Rhodnius prolixus contains at least seven homologous
Nitrophorin
Property of hemoglobin and oxygenation
The Haldane effect is a property of hemoglobin (Hb) that describes its ability to carry increased amounts of carbon dioxide (CO2) in the deoxygenated state
Haldane_effect
Protein found in humans
by a peroxidase function of the cardiolipin–cytochrome c complex. The hemoprotein is then detached from the mitochondrial inner membrane and can be extruded
Cytochrome_c
Protein family
Erythrocruorin (from Greek eruthros "red" + Latin cruor "blood"), and the similar chlorocruorin (from Greek khlōros "green" + Latin cruor "blood"), are
Erythrocruorin
Cytochrome d is, as other proteins of its family, a membrane-bound hemoprotein, but unlike cytochromes a and b, cytochrome D has a heme D instead of
Cytochrome_d
British-born biophysicist
Dyson, Helen Jane (1976). Dynamic and equilibrium spectrophotometry of hemoproteins. gov.au (PhD thesis). University of Sydney. OCLC 221180299. The Scientists'
Jane_Dyson
Superfamily of oxygen-transporting globular proteins
detoxification and in nitrosative stress. Cyanoglobin (or GlbN): a truncated hemoprotein found in cyanobacteria that has high oxygen affinity, and which appears
Globin
Medical condition
marrow and 15% in parenchymal cells in the liver, where turnover of hemoproteins is high. In AIP, over 100 mutations have been identified on the long
Acute_intermittent_porphyria
Type of thin-film solar cell
on porphyrin. In nature, porphyrin is the basic building block of the hemoproteins, which include chlorophyll in plants and hemoglobin in animals. He reports
Dye-sensitized_solar_cell
Enzyme
europaea and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins. Rees MK (January 1968). "Studies of the hydroxylamine metabolism of
Hydroxylamine_dehydrogenase
Class of proteins
1128/MCB.25.18.8044-8051.2005. PMC 1234339. PMID 16135796. Sun, J (2002). "Hemoprotein Bach1 regulates enhancer availability of heme oxygenase-1 gene". EMBO
Small_Maf
Microbiological and biochemical method for identification
possess cytochrome oxidase or indophenol oxidase (an iron-containing hemoprotein). These both catalyze the transport of electrons from donor compounds
Oxidase_test
A hemichrome (FeIII) is a form of low-spin methemoglobin (metHb). Hemichromes, which precede the denaturation processes of hemoglobin (Hb), are mainly
Hemichrome
Enzyme
The cytochrome b6f complex (plastoquinol/plastocyanin reductase or plastoquinol/plastocyanin oxidoreductase; EC 7.1.1.6) is an enzyme found in the thylakoid
Cytochrome_b6f_complex
Class of enzymes
(R)-reticuline salutaridine The enzyme is a hemoprotein of cytochrome P450 type. Enzyme 1.14.19.54 at KEGG Pathway Database.
1,2-dehydroreticuline synthase
1,2-dehydroreticuline_synthase
Change in the action or side effects of a drug caused
P450 oxidases. Cytochrome P450 is a very large family of haemoproteins (hemoproteins) that are characterized by their enzymatic activity and their role in
Drug_interaction
Chemical compound
in the release of cytochrome c. In the mitochondria, the release of hemoprotein happens through 2-step process: Firstly, the dissociation of cytochrome
Dicycloplatin
Protein and coding gene in humans
oxidoreductase activity cadmium ion binding nitric-oxide synthase activity NADPH-hemoprotein reductase activity Cellular component cytoplasm endocytic vesicle membrane
Endothelial_NOS
"Enantioselective Aminohydroxylation of Styrenyl Olefins Catalyzed by an Engineered Hemoprotein". Angewandte Chemie. 58 (10): 3138–3142. Bibcode:2019ACIE...58.3138C
Artificial_metalloenzyme
The Arc system is a two-component system found in some bacteria that regulates gene expression in facultative anaerobes such as Escheria coli. Two-component
Arc_system
flavoprotein reductase A (FprA), bacterial-type Fe3S4 ferredoxin and CYP51 hemoprotein. An unusual one-component P450 system was originally found in Rhodococcus
P450-containing_systems
6.2.2: cytochrome-b5 reductase EC 1.6.2.3: deleted EC 1.6.2.4: NADPH—hemoprotein reductase EC 1.6.2.5: NADPH—cytochrome-c2 reductase EC 1.6.2.6: leghemoglobin
List_of_EC_numbers_(EC_1)
Topics referred to by the same term
Chemical Classification System Cytochrome b5, ubiquitous electron transport hemoproteins Cytochrome b5, type A, a human microsomal cytochrome b5 HLA-B5, an HLA-B
B5
Boosting the number of red blood cells in the bloodstream
mass spectrometer allowed increased accuracy in selectivity between hemoproteins and other proteins and definite determination of HBOC uptake. The detection
Blood_doping
Oxygen-carrying phytoglobin found in rhizome of leguminous plants
Leghemoglobin (also leghaemoglobin or legoglobin) is an oxygen-carrying phytoglobin found in the nitrogen-fixing root nodules of leguminous plants. It
Leghemoglobin
Protein that contains a metal ion cofactor
Evolution of metal ions in biological systems Biometal Coenzyme Dioxygenase Hemoproteins Metalloproteinase Deoxyribozyme Siderophore Plant matrix metalloproteinase
Metalloprotein
American scientist
Bowdoin Known for Biophysics using Resonance Raman spectroscopy of hemoproteins Scientific career Fields Biophysics Institutions Albert Einstein College
Denis_Rousseau
Mammalian protein found in Homo sapiens
Cytoglobin is the protein product of CYGB, a human and mammalian gene. Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably
Cytoglobin
Substances delivering CO within the body
of heme derived CO production is attributed to hepatic catabolism of hemoproteins (myoglobin, cytochromes, catalase, peroxidases, soluble guanylate cyclase
Carbon monoxide-releasing molecules
Carbon_monoxide-releasing_molecules
Lyase enzyme that synthesizes cGMP from GTP
Guanylate cyclase (EC 4.6.1.2, also known as guanyl cyclase, guanylyl cyclase, or GC; systematic name GTP diphosphate-lyase (cyclizing; 3′,5′-cyclic-GMP-forming))
Guanylate_cyclase
Chemical compound
process, as published by the influential group of S. Yoshikawa. Heme Hemoprotein Cytochrome c oxidase (Complex IV of cellular respiration) Caughey, W
Heme_A
Protein-coding gene in the species Homo sapiens
to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). This reaction is the first common step in the biosynthesis of all biological
Delta-aminolevulinic acid dehydratase
Delta-aminolevulinic_acid_dehydratase
Metals subset of trace elements
depending on the food source. Heme iron is derived from the digestion of hemoproteins in meat. Non-heme iron is mainly derived from plants and exist as iron(II)
Trace_metal
Protein-coding gene in the species Homo sapiens
activity signaling receptor binding nitric-oxide synthase activity NADPH-hemoprotein reductase activity NADP binding Cellular component cytoplasm cytosol
Nitric oxide synthase 2 (inducible)
Nitric_oxide_synthase_2_(inducible)
Cytochrome c peroxidase, CCP, or CcP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome
Cytochrome_c_peroxidase
Canadian physicist
the University of Toronto involved spectroscopic investigations into hemoprotein. She developed ultrafast pump-probe spectroscopy to understand the dynamics
Jennifer_Ogilvie
Medical condition
17,20-lyase deficiency caused by deficiency in cytochrome b5, a small hemoprotein that acts as an allosteric factor to facilitate the interaction of CYP17A1
Cytochrome_b5_deficiency
Protein-coding gene in the species Homo sapiens
ontology Molecular function oxidoreductase activity FMN binding NADPH-hemoprotein reductase activity protein binding flavin adenine dinucleotide binding
NDOR1
reduced nicotinamide adenine dinucleotide phosphate in combination with a hemoprotein, which allows it to use molecular oxygen to oxidatively combine the alkaloid
Berbamunine_synthase
Class of enzymes
N-hydroxytyrosine + NADP+ The enzyme is a cytochrome P450 type of hemoprotein which contains reduced nicotinamide adenine dinucleotide phosphate (NADPH)
Tyrosine_N-monooxygenase
Class of enzymes
linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein". The Journal of Biological Chemistry. 271 (24): 14112–8. doi:10.1074/jbc
9,12-octadecadienoate 8-hydroperoxide 8S-isomerase
9,12-octadecadienoate_8-hydroperoxide_8S-isomerase
Takai K, Ushiro H, Noda Y, Narumiya S, Tokuyama T (1977). "Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan
Tryptophan_2'-dioxygenase
linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein". The Journal of Biological Chemistry. 271 (24): 14112–8. doi:10.1074/jbc
Linoleate_8R-lipoxygenase
Protein complexes present on the cell membranes of bacteria for secretion of substances
crucial role in bacterial heme acquisition by binding heme from host hemoproteins and transferring it to TonB-dependent receptors for iron uptake. The
Bacterial_secretion_system
Protein family
Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative
Haem_peroxidase
Protein-coding gene in the species Homo sapiens
dinucleotide binding arginine binding nitric-oxide synthase activity NADPH-hemoprotein reductase activity Cellular component membrane photoreceptor inner segment
NOS1
Enzyme found in humans
aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein". The Journal of Biological Chemistry. 258 (5): 3285–3293. doi:10
Prostacyclin_synthase
(November 1975). "Proceedings: Proton magnetic relaxation of some high spin hemoproteins in aqueous solutions". Israel Journal of Medical Sciences. 11 (11): 1185
Female gangs in the United States
Female_gangs_in_the_United_States
Heme protein transcription factor
relatively low-affinity DNA binding, whereas RcoM-2 is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch, resulting in high-affinity
Regulator_of_CO_metabolism
Group of bacterial ferritin proteins that protect DNA against oxidative damage
ferritin cages have also been used to encapsulate enzymes. Cytochrome C, a hemoprotein with peroxidase-like activity when encapsulated inside Dps cage showed
DNA-binding protein from starved cells
DNA-binding_protein_from_starved_cells
Chemical compound
exhibited a 2 nanometer blue shift in the Soret maximum for the reduced hemoprotein-CO complex. Cytochrome P450c and cytochrome P450d were significantly
Heptachlorodibenzo-p-dioxin
Metmyoglobin is the oxidized form of the oxygen-carrying hemeprotein myoglobin. Metmyoglobin is the cause of the characteristic brown colouration of meat
Metmyoglobin
Chemical compound
Fetherston, J. D. (2003). "Yersinia pestis TonB: Role in Iron, Heme, and Hemoprotein Utilization". Infection and Immunity. 71 (7): 4159–4162. doi:10.1128/IAI
Yersiniabactin
linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein". J. Biol. Chem. 271 (24): 14112–8. doi:10.1074/jbc.271.24.14112. PMID 8662736
Linoleate_diol_synthase
Class of enzymes
PMID 13426111. Fujita T, Mannering GJ (1971). "Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene"
Unspecific_monooxygenase
Human enzyme
CYP4F2 is a member of the cytochrome P450 (CYP) superfamily, a group of hemoprotein enzymes bound to cell membranes that are most abundant in the liver.
CYP4F2
Protein family
24S-hydroxycholesterol + NADP+ The four substrates of this enzyme are cholesterol, a hemoprotein-bound nicotinamide adenine dinucleotide phosphate (NADPH), oxygen, and
Cholesterol_24-hydroxylase
Class of neurotransmitters
interacting with ferrous ion complexes such as the prosthetic heme moiety of hemoproteins. Aside from Fe2+ interactions, CO may also interact with zinc within
Gasotransmitter
Moldovan-American theoretical physicist
Stavrov, S. S. (1988). "Structure and properties of metalloporphyrins and hemoproteins: the vibronic approach". Coordination Chemistry Reviews. 88: 1–68. doi:10
Isaac_B._Bersuker
Set of cytochrome P450 enzymes
endoplasmic reticulum-bound) enzymes contain a heme cofactor and therefore are hemoproteins. The superfamily comprises more than 11,000 genes categorized into 1
Epoxygenase
Scottish professor and researcher of pharmacology
of the CYP74 family of cytochrome P450s, and on the catalase-related hemoproteins which also metabolize fatty acid hydroperoxides. As of 2023[update],
Alan_Brash_(pharmacologist)
Nanostructures of protein-polymer conjugates
Takashi (2012-02-14). "Chemically Programmed Supramolecular Assembly of Hemoprotein and Streptavidin with Alternating Alignment". Angewandte Chemie. 124
Polymer-protein_hybrid
HEMOPROTEIN
HEMOPROTEIN
HEMOPROTEIN
HEMOPROTEIN
Boy/Male
Indian, Punjabi, Sikh
Lord Krishna's Love or the Love for Lord Krishna
Boy/Male
Australian, Indian, Kannada, Srilankan
Brilliant
Boy/Male
Tamil
Jayaganesh | ஜயகணேஷ
Victory person
Girl/Female
German
Boldest
Boy/Male
German
Dominant Ruler
Boy/Male
American, Anglo, Australian, British, Chinese, Christian, English, French, German, Jamaican
Pleasant Stone; Town of Victory; From the Friend's Town; Wine's Town; Joyful Stone; Homestead
Girl/Female
Indian
Beautiful, Radiant
Girl/Female
Indian
Assisted, Victorious
Girl/Female
Australian, Irish
Sea Child; Born of the Sea
Biblical
fruits or prophecies of judgment
HEMOPROTEIN
HEMOPROTEIN
HEMOPROTEIN
HEMOPROTEIN
HEMOPROTEIN