Regulation of FNR dimerization by subunit charge repulsion. (Q54456167)

30 May 2018

title

Regulation of FNR dimerization by subunit charge repulsion. (English)

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30 May 2018

author name string

Laura J Moore

series ordinal

1

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30 May 2018

Erin L Mettert

series ordinal

2

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30 May 2018

Patricia J Kiley

series ordinal

3

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30 May 2018

language of work or name

English

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publication date

7 September 2006

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30 May 2018

Journal of Biological Chemistry

published in

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volume

281

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page(s)

33268-33275

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issue

44

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30 May 2018

DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen.

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

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CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein

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Characterization of the dimerization domain in the FNR transcription factor.

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The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state.

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Characterization of FNR* mutant proteins indicates two distinct mechanisms for altering oxygen regulation of the Escherichia coli transcription factor FNR.

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The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli

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21 January 2018

Identifiers

DOI

10.1074/JBC.M608331200

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30 May 2018

PubMed ID

16959764

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30 May 2018