Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1 (Q27644610)

1

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Lluis Masip

Lluis Masip

4

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Hideaki Unno

Hideaki Unno

2

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José M Gualberto

José Manuel Gualberto

7

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Jean-Pierre Jacquot

Jean-Pierre Jacquot

14

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author name string

Sibali Bandyopadhyay

3

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Sung-Kun Kim

5

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Masakazu Hirasawa

6

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Virginie Lattard

8

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Masami Kusunoki

9

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David B Knaff

10

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George Georgiou

11

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Toshiharu Hase

12

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Michael K Johnson

Proceedings of the National Academy of Sciences of the United States of America

13

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language of work or name

English

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publication date

1 May 2007

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published in

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volume

104

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issue

18

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page(s)

7379-84

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cites work

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Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster

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Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p

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Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes

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Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism

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Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system

20 March 2017

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Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria

20 March 2017

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Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis

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A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm

29 September 2017

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Biogenesis of iron-sulfur proteins in plants

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Plant glutaredoxins: still mysterious reducing systems

29 September 2017

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The Tat protein translocation pathway and its role in microbial physiology

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Protein disulfide bond formation in prokaryotes

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The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm

29 September 2017

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Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

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Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli

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NMR reveals a novel glutaredoxin-glutaredoxin interaction interface

29 September 2017

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Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein

2 June 2018

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Resonance Raman studies of Rieske-type proteins

2 June 2018

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An engineered pathway for the formation of protein disulfide bonds

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Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro

21 January 2018

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Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria.

21 January 2018

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Human ferrochelatase is an iron-sulfur protein.

21 January 2018

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Characterization of the cofactor composition of Escherichia coli biotin synthase

21 January 2018

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Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster.

21 January 2018

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Protein measurement using bicinchoninic acid: elimination of interfering substances

21 January 2018

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IscU as a Scaffold for Iron−Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscU†

21 January 2018

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Structural Insight into Poplar Glutaredoxin C1 with a Bridging Iron−Sulfur Cluster at the Active Site†,‡

21 January 2018

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Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo.

27 November 2018

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Oxidation-reduction properties of disulfide-containing proteins of the Rhodobacter capsulatus cytochrome c biogenesis system

27 November 2018

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12 December 2020

Circular dichroism and magnetic circular dichroism of iron-sulfur proteins

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12 December 2020

Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples

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Resonance Raman and magnetic circular dichroism studies of reduced [2Fe-2S] proteins

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Identifiers

DOI

10.1073/PNAS.0702268104

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3383577

ADS bibcode

2007PNAS..104.7379R

0 references

OpenCitations bibliographic resource ID

3383577

1 reference