Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I (Q27620642)

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V Sridhar

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G S Prasad

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C D Stout

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F A Armstrong

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B K Burgess

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

17 December 1999

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published in

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volume

274

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issue

51

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page(s)

36479-87

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Oxidation-reduction properties of several low potential iron-sulfur proteins and of methylviologen

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Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35 A resolution and determination of the [Fe-S] bonds with 0.01 A accuracy

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Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster

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Calculation of the redox potentials of iron-sulfur proteins: the 2-/3-couple of [Fe4S*4Cys4] clusters in Peptococcus aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein.

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Overexpression of ferredoxin I in Azotobacter vinelandii

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Circular dichroism and magnetic circular dichroism of Azotobacter vinelandii ferredoxin I.

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A T14C variant of Azotobacter vinelandii ferredoxin I undergoes facile [3Fe-4S]0 to [4Fe-4S]2+ conversion in vitro but not in vivo

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Characterization of an autoreduction pathway for the [Fe4S4]3+ cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center

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Effect of replacing conserved proline residues on the EPR and NMR properties of Clostridium pasteurianum 2[4Fe-4S] ferredoxin

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On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe-4S] ferredoxin

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release_j33qynygerav5jwn27f42as4l4

21 January 2018

Identifiers

DOI

10.1074/JBC.274.51.36479

0 references

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/j33qynygerav5jwn27f42as4l4