14875-96-8Relevant articles and documents
Characterisation of Desulfovibrio vulgaris haem b synthase, a radical SAM family member
Lobo, Susana A.L.,Lawrence, Andrew D.,Rom?o, Célia V.,Warren, Martin J.,Teixeira, Miguel,Saraiva, Lígia M.
, p. 1238 - 1247 (2014)
An alternative route for haem b biosynthesis is operative in sulfate-reducing bacteria of the Desulfovibrio genus and in methanogenic Archaea. This pathway diverges from the canonical one at the level of uroporphyrinogen III and progresses via a distinct branch, where sirohaem acts as an intermediate precursor being converted into haem b by a set of novel enzymes, named the alternative haem biosynthetic proteins (Ahb). In this work, we report the biochemical characterisation of the Desulfovibrio vulgaris AhbD enzyme that catalyses the last step of the pathway. Mass spectrometry analysis showed that AhbD promotes the cleavage of S-adenosylmethionine (SAM) and converts iron-coproporphyrin III via two oxidative decarboxylations to yield haem b, methionine and the 5′-deoxyadenosyl radical. Electron paramagnetic resonance spectroscopy studies demonstrated that AhbD contains two [4Fe-4S]2 +/1 + centres and that binding of the substrates S-adenosylmethionine and iron-coproporphyrin III induces conformational modifications in both centres. Amino acid sequence comparisons indicated that D. vulgaris AhbD belongs to the radical SAM protein superfamily, with a GGE-like motif and two cysteine-rich sequences typical for ligation of SAM molecules and iron-sulfur clusters, respectively. A structural model of D. vulgaris AhbD with putative binding pockets for the iron-sulfur centres and the substrates SAM and iron-coproporphyrin III is discussed.
The Moessbauer Spectrum of an Intermediate Spin (S = 1) Four-co-ordinated (Protoporphyrinato IX)Iron(II) Complex in a Frozen Aqueous Solution of Cetyltrimethylammonium Bromide
Medhi, Okhil K.,Silver, Jack
, p. 1199 - 1200 (1989)
The Moessbauer spectrum of the four-co-ordinated haem, (protoporphyrinato IX)iron(II) monodispersed in an aqueous detergent solution of 5percent cetyltrimethylammonium bromide (CTAB), is that of a typical intermediate spin (S = 1) system -1 and the quadrupole splitting (ΔEQ) is 1.44(2) mm s-1>; the results are comparable to those found in synthetic (porphyrinato)iron(II) analogues, the ΔEQ values follow the ? donating ability (basicity) of the porphyrin ligands and the two lines of the quadrupole doublet are of unequal intensity at 78 K.
Hansen, Patricia A.,Moore, John N.,Hochstrasser, Robin M.
, p. 49 - 62 (1989)
Ahmet, Mustafa T.,Al-Jaff, Golzar,Silver, Jack,Wilson, Michael T.
, p. 43 - 50 (1991)
Heme activates artemisinin more efficiently than hemin, inorganic iron, or hemoglobin
Zhang, Shiming,Gerhard, Glenn S.
, p. 7853 - 7861 (2008)
Artemisinin derivatives appear to mediate their anti-malarial through an initial redox-mediated reaction. Heme, inorganic iron, and hemoglobin have all been implicated as the key molecules that activate artemisinins. The reactions of artemisinin with diff
A METHOD FOR PREPARING SOY LEGHEMOGLOBIN USING ESCHERICHIA COLI
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Paragraph 00101-00102, (2021/07/17)
A method for preparing a soy leghemoglobin includes: constructing a first plasmid containing genes for heme biosynthesis pathway enzymes; constructing a second plasmid containing gene for Glycine max leghemoglobin LGB2; constructing a first Escherichia coli production host containing the first plasmid and the second plasmid; and producing the soy leghemoglobin by culturing the first Escherichia coli production host. A composition useful as a meat flavor and/or an iron supplement includes the soy leghemoglobin prepared in accordance with the method.
CHEMICAL METHOD FOR PREPARING HEME IRON NOT DERIVED FROM PORCINE BLOOD
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Paragraph 0037-0039; 0051; 0053; 0055, (2019/11/22)
The present invention relates to heme iron not derived from porcine blood and a method of preparing the same, and more particularly to a method of chemically preparing heme iron not derived from porcine blood, a method of preparing a salt thereof, and an iron supplement containing the salt thus prepared as an active ingredient.
