GlutaredoxinV1, Main, Exploration, bibRecord, 000314

Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry.

Identifieur interne : 000314 ( Main/Exploration ); précédent : 000313; suivant : 000315

Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry.

Auteurs : Sambuddha Sen [États-Unis] ; J A Cowan [États-Unis]

Source :

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [ 1432-1327 ] ; 2017.

RBID : pubmed:28836015

Descripteurs français

English descriptors

KwdEn :
- Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione (chemistry), Glutathione (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Kinetics (MeSH), Ligands (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Stereoisomerism (MeSH).
MESH :
- chemical , chemistry : Glutaredoxins, Glutathione, Iron-Sulfur Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutaredoxins, Glutathione, Iron-Sulfur Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemistry : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Kinetics, Ligands, Stereoisomerism.

Abstract

Monothiol glutaredoxins (Grx) serve as intermediate cluster carriers in iron-sulfur cluster trafficking. The [2Fe-2S]-bound holo forms of Grx proteins display cysteinyl coordination from exogenous glutathione (GSH), in addition to contact from protein-derived Cys. Herein, we report mechanistic studies that investigate the role of exogenous glutathione in defining cluster chirality, ligand exchange, and the cluster transfer chemistry of Saccharomyces cerevisiae Grx3. Systematic perturbations were introduced to the glutathione-binding site by substitution of conserved charged amino acids that form crucial electrostatic contacts with the glutathione molecule. Native Grx3 could also be reconstituted in the absence of glutathione, with either DTT, BME or free L-cysteine as the source of the exogenous Fe-S ligand contact, while retaining full functional reactivity. The delivery of the [2Fe-2S] cluster to Grx3 from cluster donor proteins such as Isa, Nfu, and a [2Fe-2S](GS)₄ complex, revealed that electrostatic contacts are of key importance for positioning the exogenous glutathione that in turn influences the chiral environment of the cluster. All Grx3 derivatives were reconstituted by standard chemical reconstitution protocols and found to transfer cluster to apo ferredoxin 1 (Fdx1) at rates comparable to native protein, even when using DTT, BME or free L-cysteine as a thiol source in place of GSH during reconstitution. Kinetic analysis of cluster transfer from holo derivatives to apo Fdx1 has led to a mechanistic model for cluster transfer chemistry of native holo Grx3, and identification of the likely rate-limiting step for the reaction.

DOI: 10.1007/s00775-017-1485-9
PubMed: 28836015

Affiliations:

États-Unis

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Le document en format XML

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<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Kinetics (MeSH)</term>
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<term>Oxidoreductases (chemistry)</term>
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<term>Saccharomyces cerevisiae (chemistry)</term>
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<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (composition chimique)</term>
<term>Glutathion (métabolisme)</term>
<term>Ligands (MeSH)</term>
<term>Oxidoreductases (composition chimique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (composition chimique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
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<term>Oxidoreductases</term>
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<term>Saccharomyces cerevisiae</term>
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<term>Glutathion</term>
<term>Oxidoreductases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
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<term>Ligands</term>
<term>Stereoisomerism</term>
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<front><div type="abstract" xml:lang="en">Monothiol glutaredoxins (Grx) serve as intermediate cluster carriers in iron-sulfur cluster trafficking. The [2Fe-2S]-bound holo forms of Grx proteins display cysteinyl coordination from exogenous glutathione (GSH), in addition to contact from protein-derived Cys. Herein, we report mechanistic studies that investigate the role of exogenous glutathione in defining cluster chirality, ligand exchange, and the cluster transfer chemistry of Saccharomyces cerevisiae Grx3. Systematic perturbations were introduced to the glutathione-binding site by substitution of conserved charged amino acids that form crucial electrostatic contacts with the glutathione molecule. Native Grx3 could also be reconstituted in the absence of glutathione, with either DTT, BME or free L-cysteine as the source of the exogenous Fe-S ligand contact, while retaining full functional reactivity. The delivery of the [2Fe-2S] cluster to Grx3 from cluster donor proteins such as Isa, Nfu, and a [2Fe-2S](GS)<sub>4</sub>
 complex, revealed that electrostatic contacts are of key importance for positioning the exogenous glutathione that in turn influences the chiral environment of the cluster. All Grx3 derivatives were reconstituted by standard chemical reconstitution protocols and found to transfer cluster to apo ferredoxin 1 (Fdx1) at rates comparable to native protein, even when using DTT, BME or free L-cysteine as a thiol source in place of GSH during reconstitution. Kinetic analysis of cluster transfer from holo derivatives to apo Fdx1 has led to a mechanistic model for cluster transfer chemistry of native holo Grx3, and identification of the likely rate-limiting step for the reaction.</div>
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<Abstract><AbstractText>Monothiol glutaredoxins (Grx) serve as intermediate cluster carriers in iron-sulfur cluster trafficking. The [2Fe-2S]-bound holo forms of Grx proteins display cysteinyl coordination from exogenous glutathione (GSH), in addition to contact from protein-derived Cys. Herein, we report mechanistic studies that investigate the role of exogenous glutathione in defining cluster chirality, ligand exchange, and the cluster transfer chemistry of Saccharomyces cerevisiae Grx3. Systematic perturbations were introduced to the glutathione-binding site by substitution of conserved charged amino acids that form crucial electrostatic contacts with the glutathione molecule. Native Grx3 could also be reconstituted in the absence of glutathione, with either DTT, BME or free L-cysteine as the source of the exogenous Fe-S ligand contact, while retaining full functional reactivity. The delivery of the [2Fe-2S] cluster to Grx3 from cluster donor proteins such as Isa, Nfu, and a [2Fe-2S](GS)<sub>4</sub>
 complex, revealed that electrostatic contacts are of key importance for positioning the exogenous glutathione that in turn influences the chiral environment of the cluster. All Grx3 derivatives were reconstituted by standard chemical reconstitution protocols and found to transfer cluster to apo ferredoxin 1 (Fdx1) at rates comparable to native protein, even when using DTT, BME or free L-cysteine as a thiol source in place of GSH during reconstitution. Kinetic analysis of cluster transfer from holo derivatives to apo Fdx1 has led to a mechanistic model for cluster transfer chemistry of native holo Grx3, and identification of the likely rate-limiting step for the reaction.</AbstractText>
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Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry.

Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry.

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