GlutaredoxinV1, Main, Exploration, bibRecord, 000D24

Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis.

Identifieur interne : 000D24 ( Main/Exploration ); précédent : 000D23; suivant : 000D25

Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis.

Auteurs : Sung-Kun Kim [États-Unis] ; Afroza Rahman ; Richard C. Conover ; Michael K. Johnson ; Jeremy T. Mason ; Varinnia Gomes ; Masakazu Hirasawa ; Mace L. Moore ; Thomas Leustek ; David B. Knaff

Source :

Biochemistry [ 0006-2960 ] ; 2006.

RBID : pubmed:16605269

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Catalysis (MeSH), Chlorophyta (chemistry), Chlorophyta (enzymology), Chlorophyta (metabolism), Cysteine (chemistry), Cysteine (metabolism), Enzyme Activation (MeSH), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases Acting on Sulfur Group Donors (chemistry), Protein Structure, Tertiary (MeSH), Sequence Alignment (MeSH), Spectrum Analysis, Raman (MeSH).
MESH :
- chemical , chemistry : Cysteine, Iron-Sulfur Proteins, Oxidoreductases Acting on Sulfur Group Donors.
- chemistry : Chlorophyta.
- enzymology : Chlorophyta.
- metabolism : Chlorophyta, Cysteine, Iron-Sulfur Proteins.
- Amino Acid Sequence, Catalysis, Enzyme Activation, Molecular Sequence Data, Mutagenesis, Site-Directed, Oxidation-Reduction, Protein Structure, Tertiary, Sequence Alignment, Spectrum Analysis, Raman.

Abstract

The 5'-adenylyl sulfate (APS) reductase from the marine macrophytic green alga Enteromorpha intestinalis uses reduced glutathione as the electron donor for the reduction of APS to 5'-AMP and sulfite. The E. intestinalis enzyme (EiAPR) is composed of a reductase domain and a glutaredoxin-like C-terminal domain. The enzyme contains a single [4Fe-4S] cluster as its sole prosthetic group. Three of the enzyme's eight cysteine residues (Cys166, Cys257, and Cys260) serve as ligands to the iron-sulfur cluster. Site-directed mutagenesis experiments and resonance Raman spectroscopy are consistent with the presence of a cluster in which only three of the four ligands to the cluster irons contributed by the protein are cysteine residues. Site-directed mutagenesis experiments suggest that the thiol group of Cys250, a residue found only in algal APS reductases, is not an absolute requirement for activity. The other four cysteines that do not serve as cluster ligands, all of which are required for activity, are involved in the formation of two redox-active disulfide/dithiol couples. The couple involving Cys342 and Cys345 has an E(m) value at pH 7.0 of -140 mV, and the one involving Cys165 and Cys285 has an E(m) value at pH 7.0 of -290 mV. The C-terminal portion of EiAPR, expressed separately, exhibits the cystine reductase activity characteristic of glutaredoxins. It is proposed that the Cys342-Cys345 disulfide provides the site for entry of electrons from reduced glutathione and that the Cys166-Cys285 disulfide may serve as a structural element that is essential for keeping the enzyme in the catalytically active conformation.

DOI: 10.1021/bi0519250
PubMed: 16605269

Affiliations:

États-Unis

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Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, USA.</nlm:affiliation>
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<author><name sortKey="Rahman, Afroza" sort="Rahman, Afroza" uniqKey="Rahman A" first="Afroza" last="Rahman">Afroza Rahman</name>
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<author><name sortKey="Conover, Richard C" sort="Conover, Richard C" uniqKey="Conover R" first="Richard C" last="Conover">Richard C. Conover</name>
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<author><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
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<author><name sortKey="Mason, Jeremy T" sort="Mason, Jeremy T" uniqKey="Mason J" first="Jeremy T" last="Mason">Jeremy T. Mason</name>
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<author><name sortKey="Gomes, Varinnia" sort="Gomes, Varinnia" uniqKey="Gomes V" first="Varinnia" last="Gomes">Varinnia Gomes</name>
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<author><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name>
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<author><name sortKey="Leustek, Thomas" sort="Leustek, Thomas" uniqKey="Leustek T" first="Thomas" last="Leustek">Thomas Leustek</name>
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<author><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name>
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<series><title level="j">Biochemistry</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Catalysis (MeSH)</term>
<term>Chlorophyta (chemistry)</term>
<term>Chlorophyta (enzymology)</term>
<term>Chlorophyta (metabolism)</term>
<term>Cysteine (chemistry)</term>
<term>Cysteine (metabolism)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (chemistry)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Spectrum Analysis, Raman (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term>
<term>Alignement de séquences (MeSH)</term>
<term>Analyse spectrale Raman (MeSH)</term>
<term>Catalyse (MeSH)</term>
<term>Chlorophyta (composition chimique)</term>
<term>Chlorophyta (enzymologie)</term>
<term>Chlorophyta (métabolisme)</term>
<term>Cystéine (composition chimique)</term>
<term>Cystéine (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Oxidoreductases acting on sulfur group donors (composition chimique)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term>
<term>Iron-Sulfur Proteins</term>
<term>Oxidoreductases Acting on Sulfur Group Donors</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Chlorophyta</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Chlorophyta</term>
<term>Cystéine</term>
<term>Ferrosulfoprotéines</term>
<term>Oxidoreductases acting on sulfur group donors</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Chlorophyta</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Chlorophyta</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chlorophyta</term>
<term>Cysteine</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chlorophyta</term>
<term>Cystéine</term>
<term>Ferrosulfoprotéines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Catalysis</term>
<term>Enzyme Activation</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Oxidation-Reduction</term>
<term>Protein Structure, Tertiary</term>
<term>Sequence Alignment</term>
<term>Spectrum Analysis, Raman</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Alignement de séquences</term>
<term>Analyse spectrale Raman</term>
<term>Catalyse</term>
<term>Données de séquences moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Oxydoréduction</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The 5'-adenylyl sulfate (APS) reductase from the marine macrophytic green alga Enteromorpha intestinalis uses reduced glutathione as the electron donor for the reduction of APS to 5'-AMP and sulfite. The E. intestinalis enzyme (EiAPR) is composed of a reductase domain and a glutaredoxin-like C-terminal domain. The enzyme contains a single [4Fe-4S] cluster as its sole prosthetic group. Three of the enzyme's eight cysteine residues (Cys166, Cys257, and Cys260) serve as ligands to the iron-sulfur cluster. Site-directed mutagenesis experiments and resonance Raman spectroscopy are consistent with the presence of a cluster in which only three of the four ligands to the cluster irons contributed by the protein are cysteine residues. Site-directed mutagenesis experiments suggest that the thiol group of Cys250, a residue found only in algal APS reductases, is not an absolute requirement for activity. The other four cysteines that do not serve as cluster ligands, all of which are required for activity, are involved in the formation of two redox-active disulfide/dithiol couples. The couple involving Cys342 and Cys345 has an E(m) value at pH 7.0 of -140 mV, and the one involving Cys165 and Cys285 has an E(m) value at pH 7.0 of -290 mV. The C-terminal portion of EiAPR, expressed separately, exhibits the cystine reductase activity characteristic of glutaredoxins. It is proposed that the Cys342-Cys345 disulfide provides the site for entry of electrons from reduced glutathione and that the Cys166-Cys285 disulfide may serve as a structural element that is essential for keeping the enzyme in the catalytically active conformation.</div>
</front>
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<ArticleTitle>Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis.</ArticleTitle>
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<Abstract><AbstractText>The 5'-adenylyl sulfate (APS) reductase from the marine macrophytic green alga Enteromorpha intestinalis uses reduced glutathione as the electron donor for the reduction of APS to 5'-AMP and sulfite. The E. intestinalis enzyme (EiAPR) is composed of a reductase domain and a glutaredoxin-like C-terminal domain. The enzyme contains a single [4Fe-4S] cluster as its sole prosthetic group. Three of the enzyme's eight cysteine residues (Cys166, Cys257, and Cys260) serve as ligands to the iron-sulfur cluster. Site-directed mutagenesis experiments and resonance Raman spectroscopy are consistent with the presence of a cluster in which only three of the four ligands to the cluster irons contributed by the protein are cysteine residues. Site-directed mutagenesis experiments suggest that the thiol group of Cys250, a residue found only in algal APS reductases, is not an absolute requirement for activity. The other four cysteines that do not serve as cluster ligands, all of which are required for activity, are involved in the formation of two redox-active disulfide/dithiol couples. The couple involving Cys342 and Cys345 has an E(m) value at pH 7.0 of -140 mV, and the one involving Cys165 and Cys285 has an E(m) value at pH 7.0 of -290 mV. The C-terminal portion of EiAPR, expressed separately, exhibits the cystine reductase activity characteristic of glutaredoxins. It is proposed that the Cys342-Cys345 disulfide provides the site for entry of electrons from reduced glutathione and that the Cys166-Cys285 disulfide may serve as a structural element that is essential for keeping the enzyme in the catalytically active conformation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>Sung-Kun</ForeName>
<Initials>SK</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Conover</LastName>
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<ForeName>Michael K</ForeName>
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<Initials>JT</Initials>
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<ForeName>Varinnia</ForeName>
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<Initials>DB</Initials>
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<Language>eng</Language>
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<Acronym>GM</Acronym>
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<Country>United States</Country>
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<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
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<MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName>
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<name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name>
<name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
<name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name>
<name sortKey="Leustek, Thomas" sort="Leustek, Thomas" uniqKey="Leustek T" first="Thomas" last="Leustek">Thomas Leustek</name>
<name sortKey="Mason, Jeremy T" sort="Mason, Jeremy T" uniqKey="Mason J" first="Jeremy T" last="Mason">Jeremy T. Mason</name>
<name sortKey="Moore, Mace L" sort="Moore, Mace L" uniqKey="Moore M" first="Mace L" last="Moore">Mace L. Moore</name>
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<country name="États-Unis"><noRegion><name sortKey="Kim, Sung Kun" sort="Kim, Sung Kun" uniqKey="Kim S" first="Sung-Kun" last="Kim">Sung-Kun Kim</name>
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       | NlmPubMed2Wicri -a GlutaredoxinV1

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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis.

Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5'-adenylyl sulfate reductase from Enteromorpha intestinalis.

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