Heme
Thus cytochrome oxidase, which has two A hemes (heme a and heme a3) in its structure, contains two moles of heme A per mole ... The most common type is heme B; other important types include heme A and heme C. Isolated hemes are commonly designated by ... Heme S is related to heme B by having a formal group at position 2 in place of the 2-vinyl group. Heme S is found in the ... Cytochrome bc1, with hemes bH, bL, and c1, contains heme B and heme C in a 2:1 ratio. The practice seems to have originated in ...
Heme transporter
A heme transporter is a protein that delivers heme to the various parts of a biological cell that require it. Heme is a major ... It appears to protect cells at the CFU-E stage by exporting heme to prevent heme toxicity. Rare homozygous mutations result in ... Members of the SLC48 and SLC49 solute carrier family participate in heme transport across cellular membranes (heme-transporting ... It is likely that heme is tightly regulated for two reasons: the toxic nature of iron in cells, and the lack of a regulated ...
Heme O
... , found in the bacterium Escherichia coli, functions in a similar manner to heme A in mammalian oxygen reduction. Heme ... Heme O (or haem O) differs from the closely related heme A by having a methyl group at ring position 8 instead of the formyl ... Heme o3 and CuB(II) in Escherichia coli Quinol Oxidase, Cytochrome bo3: MCD and EPR Studies". J. Am. Chem. Soc. 126 (13): 4157- ...
Heme A
... is similar to heme o, in that both have this farnesyl addition at position 2 but heme O does not have the formyl group ... Like heme B, heme A is often attached to the apoprotein through a coordinate bond between the heme iron and a conserved amino ... is a structural relative of heme B, a component of hemoglobin, the red pigment in blood. Heme A differs from heme B in that a ... Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron ...
Heme oxygenase
"Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis". The ... Unlike HO-1, HO-2 is a hemoprotein containing heme regulatory motifs that contain heme independent of the heme catabolic site. ... originating from heme via heme oxygenase and ~14% from non-heme sources including: photooxidation, lipid and keto acid ... There are many heme degrading enzymes in nature. In general, only aerobic heme degrading enzymes are referred to as HMOX-like ...
Heme arginate
... (or haem arginate) is a compound of heme and arginine used in the treatment of acute porphyrias. This heme ... Heme arginate is a heme compound, whereby L-arginine is added to prevent rapid degradation. It is given intravenously, and its ... Volin, L; V Rasi; E Vahtera; R Tenhunen (1988). "Heme arginate: effects on hemostasis" (PDF). Blood. 71 (3): 625-628. doi: ...
Heme C
... (or haem C) is an important kind of heme. The correct structure of heme C was published, in mid 20th century, by the ... Heme C differs from heme B in that the two vinyl side chains of heme B are replaced by covalent, thioether linkages to the ... doi:10.1021/ar970084p.{{cite journal}}: CS1 maint: multiple names: authors list (link) Heme Protoporphyrin IX Heme A Heme B ... The structure of heme C, based upon NMR and IR experiments of the reduced, Fe(II), form of the heme, was confirmed in 1975. The ...
Heme B
... or haem B (also known as protoheme IX) is the most abundant heme. Hemoglobin and myoglobin are examples of oxygen ... The correct structures of heme B and heme S were first elucidated by German chemist Hans Fischer. Ogun, Aminat S.; Joy, Neena V ... also contain heme B at one of two active sites. Generally, heme B is attached to the surrounding protein matrix (known as the ... transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes ( ...
Heme ligase
... (EC 4.99.1.8, heme detoxification protein, HDP, hemozoin synthase) is an enzyme with systematic name Fe3+: ... Heme+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 4.99.1). ... Jani D, Nagarkatti R, Beatty W, Angel R, Slebodnick C, Andersen J, Kumar S, Rathore D (April 2008). "HDP-a novel heme ... beta-hematin This heme detoxifying enzyme is found in Plasmodium parasites. ...
Heme-transporting ATPase
... and heme, whereas its 3 products are ADP, phosphate, and heme. This enzyme belongs to the family of hydrolases, specifically ... In enzymology, a heme-transporting ATPase (EC 3.6.3.41) is an enzyme that catalyzes the chemical reaction ATP + H2O + hemein ... Jekabsons W, Schuster W (1995). "orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria". ... The systematic name of this enzyme class is ATP phosphohydrolase (heme-exporting). This enzyme participates in abc transporters ...
Non-heme iron protein
In biochemistry, non-heme iron proteins describe families of enzymes that utilize iron at the active site but lack heme ... Some non-heme iron proteins contain one Fe at their active sites, others have pairs of Fe centers: Many mono-Fe proteins are ... Que, Lawrence; Ho, Raymond Y. N. (1996). "Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites". Chemical ... Abu-Omar, Mahdi M.; Loaiza, Aristobulo; Hontzeas, Nikos (2005). "Reaction Mechanisms of Mononuclear Non-Heme Iron Oxygenases". ...
Animal heme-dependent peroxidases
Animal heme-dependent peroxidases is a family of peroxidases. Peroxidases are found in bacteria, fungi, plants and animals. On ... Poulos TL, Li H (1994). "Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures ... at the heme binding site. Both MPO and the catalytic domain of PGHS are mainly alpha-helical, 19 helices being identified as ... the basis of sequence similarity, a number of animal heme peroxidases can be categorized as members of a superfamily: ...
Protein metabolism
"Heme". PubChem. Retrieved 2019-02-20. López-Otín C, Bond JS (November 2008). "Proteases: multifunctional enzymes in life and ... Proteins may also incorporate other molecules such as the heme group in hemoglobin, a protein responsible for carrying oxygen ...
Coproporphyrinogen III
heme. In the main porphyrin biosynthesis pathway, coproporphyrinogen III is derived from uroporphyrinogen III by the action of ... Paul R. Ortiz de Montellano (2008). "Hemes in Biology". Wiley Encyclopedia of Chemical Biology. John Wiley & Sons. doi:10.1002/ ...
Murburn concept
Heme/flavin enzymology and electron transfer phenomena Enzymes containing heme and flavin groups (as exemplified by peroxidases ... Ecology Fungal heme haloperoxidases (like chloroperoxidase) are the ultimate source for the generation of the vast majority of ... Dunford BH (1999). Heme peroxidases. John Wiley. ISBN 0-471-24244-6. Dawson JH (April 1988). "Probing structure-function ... While several moiety and electron transfer reactions they catalyze are mediated at the active site (heme/flavin center), some ...
GATA1
... hemoglobin and heme. GATA1 plays a similarly critical role in the maturation of blood platelets from megakaryoblasts, ... contribute to the formation of their cytoskeleton and that make enzymes necessary for the biosynthesis of hemoglobins and heme ...
Cytochrome
... to visible spectroscopic signatures of hemes are still used to identify heme type from the reduced bis-pyridine-ligated state, ... The heme group is a highly conjugated ring system (which allows its electrons to be very mobile) surrounding an iron ion. The ... Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are ... They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International ...
Dioxygenase
... which are heme dioxygenases that utilize iron coordinated by a heme B prosthetic group. While these dioxygenases are of ... and those utilizing a heme prosthetic group. The mononuclear iron dioxygenases, or non-heme iron-dependent dioxygenases as they ... The other heme iron-dependent dioxygenase, IDO, also has relevance to human health, as it functions in inflammatory responses ... Efimov I, Basran J, Thackray SJ, Handa S, Mowat CG, Raven EL (April 2011). "Structure and reaction mechanism in the heme ...
Tryptophan 2,3-dioxygenase
TDO is assumed to react in the same way, but a ferryl heme has not been observed in TDO. See also discussion of mechanism for ... In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L-tryptophan (L-Trp ... This suggested a base-catalysed abstraction mechanism, involving only the ferrous (FeII) heme. It is assumed that TDO and IDO ... In IDO, a ferryl heme (FeIV) has been identified during turnover. Mechanistic proposals have therefore been adjusted to include ...
Bilirubin glucuronide
"Heme metabolism in macrophages". eClinpath. Archived from the original on 2018-05-17. Retrieved 2019-05-05. "Bilirubin and ...
Lesser Poland
Heme Oxygenases 2007 Conference. Jagiellonian University. Archived from the original on 15 July 2007. Retrieved 14 August 2007 ...
Methyltetrahydroprotoberberine 14-monooxygenase
This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme. Rueffer M, Zenk MH (1987). "Enzymatic ... Heme enzymes, Enzymes of unknown structure, All stub articles, EC 1.14.13 stubs). ...
Tryptophan alpha,beta-oxidase
Portal: Biology v t e (EC 1.3.3, Heme enzymes, Enzymes of unknown structure, All stub articles, EC 1.3 stubs). ... It employs one cofactor, heme. Genet R, Denoyelle C, Menez A (1994). "Purification and partial characterization of an amino ...
S)-limonene 7-monooxygenase
It employs one cofactor, heme. Karp F, Mihaliak CA, Harris JL, Croteau R (1990). "Monoterpene biosynthesis: specificity of the ... Heme enzymes, Enzymes of unknown structure, All stub articles, EC 1.14.13 stubs). ...
Cholesterol 7alpha-monooxygenase
It employs one cofactor, heme. Boyd GS, Grimwade AM, Lawson ME (1973). "Studies on rat-liver microsomal cholesterol 7alpha- ... Heme enzymes, Enzymes of unknown structure, All stub articles, EC 1.14.13 stubs). ...
Tryptophan 2'-dioxygenase
Portal: Biology v t e (EC 1.13.99, Heme enzymes, Enzymes of unknown structure, All stub articles, Oxidoreductase stubs). ... It employs one cofactor, heme. Roberts J, Rosenfeld HJ (1977). "Isolation, crystallization, and properties of indolyl-3-alkane ...
Linalool 8-monooxygenase
... heme. Bhattacharyya PK, Samanta TB, Ullah AH, Gunsalus IC (1984). "Chemical probes into the active centre of a heme thiolate ... Portal: Biology (EC 1.14.14, Heme enzymes, Enzymes of unknown structure). ...
Carbon monoxide-releasing molecules
... originating from heme via heme oxygenase and ~14% from non-heme sources including: photooxidation, lipid peroxidation, and ... thereby identifying the heme oxygenase (HMOX) enzyme. HMOX is a heme-containing member of the heat shock protein (HSP) family ... of heme derived endogenous CO production. The majority of the remaining 20% of heme derived CO production is attributed to ... Some PPIX analogs such as tin PPIX, tin mesoporphyrin, and zinc PPIX, are heme oxygenase inhibitors. HMOX is regarded as the ...
Isoflavone 3'-hydroxylase
doi:10.1016/0014-5793(87)80021-2. Portal: Biology v t e (EC 1.14.14, NADPH-dependent enzymes, Heme enzymes, Enzymes of unknown ... It employs one cofactor, heme. Hinderer W, Flentje U, Barz W (1987). "Microsomal isoflavone 2'-hydroxylases and 3'-hydroxylases ...
ALAS1
Diseases related to heme biosynthesis". Mol. Biol. Med. 7 (5): 405-21. PMID 2095458. Dwyer BE, Smith MA, Richardson SL, et al ... 2004). "Increased heme oxygenase-1 and decreased delta-aminolevulinate synthase expression in the liver of patients with acute ... This nuclear-encoded mitochondrial enzyme is the first and rate-limiting enzyme in the mammalian heme biosynthetic pathway. ... 2008). "Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin". Mol. Cell. Biochem. ...