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Siroheme Enzymes
Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. It is a cofactor at the active site of sulfite reductase, which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide, which can be incorporated into the organic compound homocysteine. Biosynthesis Like all tetrapyrroles, the macrocyclic ligand in siroheme is derived from uroporphyrinogen III. This porphyrinogen is methylated at two adjacent pyrrole rings to give dihydrosirohydrochlorin, which is subsequently oxidized to give sirohydrochlorin. A ferrochelatase then inserts iron into the macrocycle to give siroheme. See also * Ferredoxin-nitrite reductase * Hydrogensulfite reductase * Nitrite reductase (NAD(P)H) In enzymology, a nitrite reductase AD(P)H'' () is an enzyme that catalyzes the chemical reaction :ammonium hydroxide + 3 NAD(P)+ + H2O \rightleftharpoons nitrite + 3 NAD(P)H + 3 H+ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Siroheme
Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. It is a cofactor at the active site of sulfite reductase, which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide, which can be incorporated into the organic compound homocysteine. Biosynthesis Like all tetrapyrroles, the macrocyclic ligand in siroheme is derived from uroporphyrinogen III. This porphyrinogen is methylated at two adjacent pyrrole rings to give dihydrosirohydrochlorin, which is subsequently oxidized to give sirohydrochlorin Sirohydrochlorin is a tetrapyrrole macrocyclic metabolic intermediate in the biosynthesis of sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which cat .... A ferrochelatase then inserts iron into the macrocycle to give siroheme. See also * Ferredoxin-nitrite ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microbiology And Molecular Biology Reviews
''Microbiology and Molecular Biology Reviews'' (published as MMBR) is a peer-reviewed scientific journal published by the American Society for Microbiology The American Society for Microbiology (ASM), originally the Society of American Bacteriologists, is a professional organization for scientists who study viruses, bacteria, fungi, algae, and protozoa as well as other aspects of microbiology. It .... History The journal was established in 1937 as ''Bacteriological Reviews'' () and changed its name in 1978 to ''Microbiological Reviews'' (). It obtained its current title in 1997. References External links * Delayed open access journals Microbiology journals Publications established in 1937 English-language journals Quarterly journals American Society for Microbiology academic journals {{microbiology-journal-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sulfur Enzymes
Sulfur (or sulphur in British English) is a chemical element with the symbol S and atomic number 16. It is abundant, multivalent and nonmetallic. Under normal conditions, sulfur atoms form cyclic octatomic molecules with a chemical formula S8. Elemental sulfur is a bright yellow, crystalline solid at room temperature. Sulfur is the tenth most abundant element by mass in the universe and the fifth most on Earth. Though sometimes found in pure, native form, sulfur on Earth usually occurs as sulfide and sulfate minerals. Being abundant in native form, sulfur was known in ancient times, being mentioned for its uses in ancient India, ancient Greece, China, and ancient Egypt. Historically and in literature sulfur is also called brimstone, which means "burning stone". Today, almost all elemental sulfur is produced as a byproduct of removing sulfur-containing contaminants from natural gas and petroleum.. Downloahere The greatest commercial use of the element is the production of su ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron Enzymes
Iron () is a chemical element with symbol Fe (from la, ferrum) and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, right in front of oxygen (32.1% and 30.1%, respectively), forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust. In its metallic state, iron is rare in the Earth's crust, limited mainly to deposition by meteorites. Iron ores, by contrast, are among the most abundant in the Earth's crust, although extracting usable metal from them requires kilns or furnaces capable of reaching or higher, about higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BCE and the use of iron tools and weapons began to displace copper alloys, in some regions, only around 1200 BCE. That event is considered the transition from the Bronze Age to the Iron Age. In ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FEBS Letters
''FEBS Letters'' is a not-for-profit peer-reviewed scientific journal published on behalf of the Federation of European Biochemical Societies (FEBS) by Wiley. It covers all aspects of molecular biosciences, including molecular biology and biochemistry. The aim of the journal is to publish primary research in the form of Research Articles, Research Letters, Communications and Hypotheses, as well as secondary research in the form of Review articles. The journal also publishes a News and Views column calle"The Scientists' Forum" The editorial office of ''FEBS Letters'' is based in Heidelberg, Germany. The journal income is reinvested in science. History The initial idea of ''FEBS Letters'' as a journal for rapid communication of short reports in biochemistry, biophysics and molecular biology was proposed by the Secretary General of FEBS, W.J. Whelan, at the 4th FEBS Meeting held in Oslo in 1967. After further discussions and preparations, the first issue of ''FEBS Letters'' appeare ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitrite Reductase (NAD(P)H)
In enzymology, a nitrite reductase AD(P)H'' () is an enzyme that catalyzes the chemical reaction :ammonium hydroxide + 3 NAD(P)+ + H2O \rightleftharpoons nitrite + 3 NAD(P)H + 3 H+ The 4 substrates of this enzyme are ammonium hydroxide, NAD+, NADP+, and H2O, whereas its 4 products are nitrite, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ammonium-hydroxide:NAD(P)+ oxidoreductase. Other names in common use include nitrite reductase (reduced nicotinamide adenine dinucleotide, (phosphate)), NADH-nitrite oxidoreductase, NADPH-nitrite reductase, assimilatory nitrite reductase, nitrite reductase AD(P)H2'', and NAD(P)H2:nitrite oxidoreductase. This enzyme participates in nitrogen metabolism. It has 3 cofactors: FAD, Iron, and Siroheme. Structural studies As of late 2007, only one structure A structure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrogensulfite Reductase
In enzymology, a hydrogensulfite reductase () is an enzyme that catalyzes the chemical reaction :trithionate + acceptor + 2 H2O + OH- \rightleftharpoons 3 bisulfite + reduced acceptor The 4 substrates of this enzyme are trithionate, acceptor, H2O, and OH-, whereas its two products are bisulfite and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other acceptors. The systematic name of this enzyme class is trithionate:acceptor oxidoreductase. Other names in common use include bisulfite reductase, dissimilatory sulfite reductase, desulfoviridin, desulforubidin, desulfofuscidin, dissimilatory-type sulfite reductase, and trithionate:(acceptor) oxidoreductase. It has 4 cofactors: iron, sulfur, siroheme Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. It is a cofactor at the active site of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sirohydrochlorin
Sirohydrochlorin is a tetrapyrrole macrocyclic metabolic intermediate in the biosynthesis of sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which catalyzes the release of methane in the final step of methanogenesis. Structure Sirohydrochlorin was first isolated in the early 1970s when it was shown to be the metal-free form of the prosthetic group in the ferredoxin-nitrite reductase from spinach. Its chemical identity was established by spectroscopy and by total synthesis. Biosynthesis Sirohydrochlorin is derived from a tetrapyrrolic structural framework created by the enzymes deaminase and cosynthetase which transform aminolevulinic acid via porphobilinogen and hydroxymethylbilane to uroporphyrinogen III. The latter is the first macrocyclic intermediate common to haem, chlorophyll, sirohaem and vitamin B12. Uroporphyrinogen III is subsequently transformed by the addition of two meth ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dihydrosirohydrochlorin
Dihydrosirohydrochlorin is one of several naturally occurring tetrapyrrole macrocyclic metabolic intermediates in the biosynthesis of vitamin B12 (cobalamin). Its oxidised form, sirohydrochlorin, is precursor to sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. Further biosynthetic transformations convert sirohydrochlorin to cofactor F430 for an enzyme which catalyzes the release of methane in the final step of methanogenesis. Biosynthesis Dihydrosirohydrochlorin is derived from a tetrapyrrolic structural framework created by the enzymes deaminase and cosynthetase which transform aminolevulinic acid via porphobilinogen and hydroxymethylbilane to uroporphyrinogen III. The latter is the first macrocyclic intermediate common to haem, chlorophyll, sirohaem and vitamin B12. Uroporphyrinogen III is subsequently transformed by the addition of two methyl groups to form dihydrosirohydrochlorin. See also *Cobalamin biosynthesis *Sirohydrochlorin *Precorrin-2 dehy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Porphyrinogen
In biochemistry a porphyrinogen is a member of a class of naturally occurring compounds with a tetrapyrrole core, a macrocycle Macrocycles are often described as molecules and ions containing a ring of twelve or more atoms. Classical examples include the crown ethers, calixarenes, porphyrins, and cyclodextrins. Macrocycles describe a large, mature area of chemistry. ... of four pyrrole rings connected by four methylene bridges. - IUPAC Gold Book They can be viewed as derived from the parent compound hexahydroporphine by the substitution of various functional groups for hydrogen atoms in the outermost (20-carbon) ring. Porphyrinogens are intermediates in the biosynthesis of porphyrins, Cofactor (biochemistry), cofactors with a porphine core which are found in many enzymes and proteins including myoglobin, hemoglobin, cytochromes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Uroporphyrinogen III
Uroporphyrinogen III is a tetrapyrrole, the first macrocyclic intermediate in the biosynthesis of heme, chlorophyll, vitamin B12, and siroheme. It is a colorless compound, like other porphyrinogens. Structure The molecular structure of uroporphyrinogen III can be described as a hexahydroporphine core, where each pyrrole ring has the hydrogen atoms on its two outermost carbons replaced by an acetic acid group (, "A") and a propionic acid group (, "P"). The groups are attached in an asymmetric way: going around the macrocycle, the order is AP-AP-AP-PA. Biosynthesis and metabolism In the general porphyrin biosynthesis pathway, uroporphyrinogen III is derived from the linear tetrapyrrole preuroporphyrinogen (a substituted hydroxymethylbilane) by the action of the enzyme uroporphyrinogen-III cosynthase. The conversion entails a reversal of the last pyrrole unit (thus swapping the acetic and propionic acid groups) and a condensation reaction that closes the macrocycle by eliminati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
