Preparation and characterization of an inorganic analog for the active site of the reduced 2Fe-S* iron-sulfur proteins

1972 ◽  
Vol 94 (24) ◽  
pp. 8375-8386 ◽  
Author(s):  
Kenneth A. Rubinson ◽  
Graham Palmer
Keyword(s):  
Active Site ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins

Biophysical Characterization of Iron-Sulfur Proteins

BIO-PROTOCOL ◽  
2021 ◽  
Vol 11 (20) ◽  
Author(s):  
Bhanu Jagilinki ◽  
Irina Paluy ◽  
Alexei Tyryshkin ◽  
Vikas Nanda ◽  
Dror Noy
Keyword(s):  
Biophysical Characterization ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins

Electron self-exchange in high-potential iron-sulfur proteins. Characterization of protein I from Ectothiorhodospira vacuolata

Biochemistry ◽  
1993 ◽  
Vol 32 (47) ◽  
pp. 12887-12893 ◽  
Author(s):  
Ivano Bertini ◽  
Alain Gaudemer ◽  
Claudio Luchinat ◽  
Mario Piccioli
Keyword(s):  
High Potential ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins

Research on isc Operon in Acidithiobacillus ferrooxidans ATCC 23270

2007 ◽  
Vol 20-21 ◽  
pp. 509-512 ◽  
Author(s):  
Jian She Liu ◽  
Yan Fei Zhang ◽  
Mei Mei Geng ◽  
Jia Zeng ◽  
Guan Zhou Qiu
Keyword(s):  
Acidithiobacillus Ferrooxidans ◽  
Purification And Characterization ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur Clusters ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins

The highly conserved operon iron–sulfur cluster (iscSUA) is essential for the general biogenesis and transfer of iron–sulfur proteins in bacteria. In this study, expression, purification and characterization of the proteins of the isc operon (iscSUA) of Acidithiobacillus ferrooxidans ATCC 23270 was studied. Assembly and transfer of [Fe4S4] in vitro during the isc proteins and other iron sulfur proteins was studied in order to detect the pathway and mechanism of [Fe4S4] assembly and transfer in vivo. The [Fe4S4] cluster was successfully assembled in iron-sulfur proteins in vitro in the presence of Fe2+ and sulfide, and it was successfully transferred from IscA or IscU to iron- sulfur proteins. Our results support and extend certain models of iron-sulfur clusters assembly and transfer.

scholarly journals Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of Chlamydomonas reinhardtii Glutaredoxin 2

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 803
Author(s):  
Thomas Roret ◽  
Bo Zhang ◽  
Anna Moseler ◽  
Tiphaine Dhalleine ◽  
Xing-Huang Gao ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Structural Properties ◽  
Active Site ◽  
Fluorescent Protein ◽  
Spectroscopic Characterization ◽  
Redox Activity ◽  
Structural Factors ◽  
Oxidoreductase Activity ◽  
Iron Sulfur

Glutaredoxins (GRXs) are thioredoxin superfamily members exhibiting thiol-disulfide oxidoreductase activity and/or iron-sulfur (Fe-S) cluster binding capacities. These properties are determined by specific structural factors. In this study, we examined the capacity of the class I Chlamydomonas reinhardtii GRX2 recombinant protein to catalyze both protein glutathionylation and deglutathionylation reactions using a redox sensitive fluorescent protein as a model protein substrate. We observed that the catalytic cysteine of the CPYC active site motif of GRX2 was sufficient for catalyzing both reactions in the presence of glutathione. Unexpectedly, spectroscopic characterization of the protein purified under anaerobiosis showed the presence of a [2Fe-2S] cluster despite having a presumably inadequate active site signature, based on past mutational analyses. The spectroscopic characterization of cysteine mutated variants together with modeling of the Fe–S cluster-bound GRX homodimer from the structure of an apo-GRX2 indicate the existence of an atypical Fe–S cluster environment and ligation mode. Overall, the results further delineate the biochemical and structural properties of conventional GRXs, pointing to the existence of multiple factors more complex than anticipated, sustaining the capacity of these proteins to bind Fe–S clusters.

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