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Siroheme information


Structure of 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.[1] 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.[2]

  1. ^ Matthew J. Murphy; et al. (1974). "Siroheme: A New Prosthetic Group Participating in Six-Electron Reduction Reactions Catalyzed by Both Sulfite and Nitrite Reductases". PNAS. 71 (3): 612–616. Bibcode:1974PNAS...71..612M. doi:10.1073/pnas.71.3.612. PMC 388061. PMID 4595566.
  2. ^ Dominique Thomas; Yolande Surdin-Kerjan (1997). "Metabolism of sulfur amino acids in Saccharomyces cerevisiae". Microbiology and Molecular Biology Reviews. 61 (4): 503–532. doi:10.1128/mmbr.61.4.503-532.1997. PMC 232622. PMID 9409150.

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Siroheme

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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...

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Chlorophyll

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synthesised along a branched biosynthetic pathway that is shared with heme and siroheme. Chlorophyll synthase is the enzyme that completes the biosynthesis of...

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Sirohydrochlorin ferrochelatase

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sirohydrochlorin ferrochelatase (EC 4.99.1.4) catalyzes the following reaction: siroheme + 2H+ ⇌ {\displaystyle \rightleftharpoons } sirohydrochlorin + Fe2+ This...

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Chlorophyll a

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and is synthesised along a branched pathway that is shared with heme and siroheme. The initial steps incorporate glutamic acid into 5-aminolevulinic acid...

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Sirohaem synthase

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In molecular biology, sirohaem synthase (or siroheme synthase) (CysG) is a multi-functional enzyme with S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase...

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Uroporphyrinogen III

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intermediate in the biosynthesis of heme, chlorophyll, vitamin B12, and siroheme. It is a colorless compound, like other porphyrinogens. The molecular structure...

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Chlorophyll b

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and is synthesised along a branched pathway that is shared with heme and siroheme. The initial steps incorporate glutamic acid into 5-aminolevulinic acid...

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Porphyrin

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some use a usual chlorin ring) sirohydrochlorin (an isobacteriochlorin) siroheme iron Important cofactor in sulfur assimilation biosynthetic intermediate...

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Bacteriochlorophyll

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uroporphyrinogen III in a separate pathway that leads, for example, to siroheme, cofactor F430 and cobalamin. The common intermediate is sirohydrochlorin...

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Vitamin B12

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latter is the first macrocyclic intermediate common to heme, chlorophyll, siroheme and B12 itself. Later steps, especially the incorporation of the additional...

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Sulfite reductase

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employs two covalently coupled cofactors - an iron sulfur cluster and a siroheme - which the deliver electrons to the substrate via this coupling. The systematic...

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Sirohydrochlorin

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Sirohydrochlorin ferrochelatase an enzyme that catalyzes insertion of iron to form siroheme. Sirohydrochlorin cobaltochelatase an enzyme that catalyzes insertion of...

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Dissimilatory sulfite reductase

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1021/bi100781f. PMID 20822098. Schedel M, Vanselow M, Trüper HG (1979). "Siroheme sulfite reductase isolated from Chromatium vinosum. Purification and investigation...

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Cofactor F430

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natural tetrapyrroles, including chlorophyll, vitamin B12, phycobilins, siroheme, heme, and heme d1. It is converted to sirohydrochlorin via dihydrosirohydrochlorin...

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Desulfovibrio alcoholivorans

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that the enzyme is multimeric and contains iron in the form of Fe4S4 and siroheme. Cytochrome c3 isolated from D. gigas is dimeric with four heme groups...

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Hydrogensulfite reductase

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trithionate:(acceptor) oxidoreductase. It has 4 cofactors: iron, sulfur, siroheme, and iron-sulfur. Hatchikian EC, Zeikus JG (1983). "Characterization of...

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