Where is ferredoxin found

Bacteriological Reviews. PMC Bibcode : Natur. Acta Crystallographica D. Journal of Molecular Biology.

To be published. Structural comparisons of bacterial ferredoxins". Bruschi M, Guerlesquin F Ciurli S, Musiani F Photosynthesis Research. Fukuyama K Journal of Bioenergetics and Biomembranes. Meyer J November FEBS Letters. Phosphate budget laboratory. Geology courses. Biosynthesis of a human protein Origin of life: polyphosphate. Categories : Articles with short description Pages with broken file links Genes on human chromosome 11 Iron-sulfur proteins Photosynthesis.

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EMBO Rep 1: — Biochem Biophys Res Commun 7: — Mossessova E and Lima CD Ulpl-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol Cell 5: — Structure 6: — PubMed Article Google Scholar. J Biochem 10— Thesis, Osaka University.

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Proteins Struct Funct Genet 52— Plant Cell Physiol — Wada K, Onda M and Matsubara H Ferredoxin isolated from plant non-photosynthetic tissues: purification and characterization. Download references. You can also search for this author in PubMed Google Scholar. Correspondence to Keiichi Fukuyama. Reprints and Permissions. Fukuyama, K. Structure and Function of Plant-Type Ferredoxins.

The while the intramolecular disulfide bond in the , molecule A is shown in blue and molecule B in green. When purified at pH 5. The [3Fe-4S] form diffracted to 2.

Crystal packing in shown in red and orange , which is the same as 1sj1 , shown in blue and cyan even though the space groups are different see also corresponding side views for and.

Biological iron-sulfur Fe-S clusters are functionally versatile, modular prosthetic groups. The electronic structure and the site of iron reduction of these protein-bound cofactors account for the electron transfer function and mechanism.

This FdxB protein contains an adrenodoxin Adx like, redox-active [2Fe-2S] cluster, which plays an essential role in the de novo iron-sulfur cluster assembly ISC system. In the lattice displaying the. Each protomer binds a that is , where the and the. In the , suggesting that a rapid interprotomer electron transfer between them would be unlikely to occur.