Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase. - Wikidata - awgldk - TriplyDB

Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase.

Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase.

http://www.wikidata.org/entity/Q38315251

about

Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme The subunit structure and catalytic mechanism of the Bacillus subtilis DNA repair enzyme spore photoproduct lyase A tribute to sulfur.Structural enzymology of biotin biosynthesis.Self-sacrifice in radical S-adenosylmethionine proteins.AdoMet radical proteins--from structure to evolution--alignment of divergent protein sequences reveals strong secondary structure element conservation Radical S-adenosylmethionine enzymes.Role of the [2Fe-2S]2+ cluster in biotin synthase: mutagenesis of the atypical metal ligand arginine 260 Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli.Reductive cleavage of S-adenosylmethionine by biotin synthase from Escherichia coli.The PLP-dependent biotin synthase from Escherichia coli: mechanistic studies.The plant biotin synthase reaction. Identification and characterization of essential mitochondrial accessory protein components.Product inhibition in the radical S-adenosylmethionine family.

P2860

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P2860

Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase.

http://www.wikidata.org/entity/Q38315251

description

2000 nî lūn-bûn

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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2000年论文

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2000年论文

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name

Mutagenesis of the proposed ir ...... herichia coli biotin synthase.

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type

label

Mutagenesis of the proposed ir ...... herichia coli biotin synthase.

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Mutagenesis of the proposed ir ...... herichia coli biotin synthase.

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S0014-5793(00)01101-7

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Mutagenesis of the proposed ir ...... herichia coli biotin synthase.

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Baldwin JE

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Hewitson KS

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Roach PL

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Shaw NM

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structures of aconitase with isocitrate and nitroisocitrate bound.

Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity.

Effect of iron-sulfur cluster environment in modulating the thermodynamic properties and biological function of ferredoxin from Pyrococcus furiosus.

SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form.

Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli.

[3Fe-4S] <--> [4Fe-4S] cluster interconversion in Desulfovibrio africanus ferredoxin III: properties of an Asp14 --> Cys mutant.

Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro.

Hyperproduction of recombinant ferredoxins in escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster.

Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction.

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372-376

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10.1016/S0014-5793(00)01101-7

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2-3

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