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Iron-Sulfur Proteins: Coenzyme Q - Cytochrome C Reductase, Rieske Protein, Ferredoxin, Iron-Sulfur Protein, Hydrogenase, Nitrogenase

Iron-Sulfur Proteins: Coenzyme Q - Cytochrome C Reductase, Rieske Protein, Ferredoxin, Iron-Sulfur Protein, Hydrogenase, NitrogenaseCreator: Books LLC
Publisher: Books LLC
Category: Book

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Media: Paperback
Pages: 50
Number Of Items: 1
Shipping Weight (lbs): 0.2
Dimensions (in): 9 x 6 x 0.1

ISBN: 115562727X
Dewey Decimal Number: 549
EAN: 9781155627274

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Product Description
Purchase includes free access to book updates online and a free trial membership in the publisher's book club where you can select from more than a million books without charge. Chapters: Coenzyme Q - Cytochrome C Reductase, Rieske Protein, Ferredoxin, Iron-Sulfur Protein, Hydrogenase, Nitrogenase, Cytochrome B6f Complex, Aconitase, Rubredoxin. Excerpt: item aconitate hydratase item Aconitase family (aconitate hydratase) Aconitase (aconitate hydratase; EC 4.2.1.3) is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis -aconitate in the tricarboxylic acid cycle , a non-redox -active process. Citric acid Aconitic acid Isocitric acid Function In contrast with the majority of iron-sulfur proteins that function as electron carriers, the iron-sulfur cluster of aconitase reacts directly with an enzyme substrate. Aconitase has an active cluster, which may convert to an inactive form. Three cysteine (Cys) residues have been shown to be ligands of the centre. In the active state, the labile iron ion of the cluster is not coordinated by Cys but by water molecules. The iron-responsive element binding protein (IRE-BP) and 3-isopropylmalate dehydratase ( -isopropylmalate isomerase; EC 4.2.1.33), an enzyme catalysing the second step in the biosynthesis of leucine , are known aconitase homologues. Iron regulatory elements (IREs) constitute a family of 28-nucleotide, non-coding, stem-loop structures that regulate iron storage, heme synthesis and iron uptake. They also participate in ribosome binding and control the mRNA turnover (degradation). The specific regulator protein, the IRE-BP, binds to IREs in both 5' and 3' regions, but only to RNA in the apo form, without the Fe-S cluster. Expression of IRE-BP in cultured cells has revealed that the protein functions either as an active aconitase, when cells are iron-replete, or as an active RNA-binding protein, when cells are iron-depleted. Mutant IRE-BPs, in which any or all of the three Cys ...