Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.
Identifieur interne : 000217 ( Main/Exploration ); précédent : 000216; suivant : 000218Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.
Auteurs : Parismita Kalita [Inde] ; Harish Shukla [Inde] ; Kundlik Gadhave [Inde] ; Rajanish Giri [Inde] ; Timir Tripathi [Inde]Source :
- Archives of biochemistry and biophysics [ 1096-0384 ] ; 2018.
Descripteurs français
- KwdFr :
- 5,5'-Dithiobis(acide 2-nitro-benzoïque) (métabolisme), Animaux (MeSH), Catalyse (MeSH), Complexes multienzymatiques (composition chimique), Complexes multienzymatiques (génétique), Complexes multienzymatiques (isolement et purification), Complexes multienzymatiques (métabolisme), Conformation des protéines (effets des médicaments et des substances chimiques), Domaines protéiques (MeSH), Dépliement des protéines (effets des médicaments et des substances chimiques), Fasciola (enzymologie), Flavine adénine dinucléotide (composition chimique), Flavine adénine dinucléotide (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (isolement et purification), Glutarédoxines (métabolisme), Liaison aux protéines (MeSH), Mutation (MeSH), NADH, NADPH oxidoreductases (composition chimique), NADH, NADPH oxidoreductases (génétique), NADH, NADPH oxidoreductases (isolement et purification), NADH, NADPH oxidoreductases (métabolisme), NADP (métabolisme), Protéines d'helminthes (composition chimique), Protéines d'helminthes (génétique), Protéines d'helminthes (isolement et purification), Protéines d'helminthes (métabolisme), Stabilité protéique (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (isolement et purification), Thiorédoxines (métabolisme), Tryptophane (composition chimique), Urée (composition chimique).
- MESH :
- composition chimique : Complexes multienzymatiques, Flavine adénine dinucléotide, Glutarédoxines, NADH, NADPH oxidoreductases, Protéines d'helminthes, Thiorédoxines, Tryptophane, Urée.
- effets des médicaments et des substances chimiques : Conformation des protéines, Dépliement des protéines.
- enzymologie : Fasciola.
- génétique : Complexes multienzymatiques, Glutarédoxines, NADH, NADPH oxidoreductases, Protéines d'helminthes, Thiorédoxines.
- isolement et purification : Complexes multienzymatiques, Glutarédoxines, NADH, NADPH oxidoreductases, Protéines d'helminthes, Thiorédoxines.
- métabolisme : 5,5'-Dithiobis(acide 2-nitro-benzoïque), Complexes multienzymatiques, Flavine adénine dinucléotide, Glutarédoxines, NADH, NADPH oxidoreductases, NADP, Protéines d'helminthes, Thiorédoxines.
- Animaux, Catalyse, Domaines protéiques, Liaison aux protéines, Mutation, Stabilité protéique.
English descriptors
- KwdEn :
- Animals (MeSH), Catalysis (MeSH), Dithionitrobenzoic Acid (metabolism), Fasciola (enzymology), Flavin-Adenine Dinucleotide (chemistry), Flavin-Adenine Dinucleotide (metabolism), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (isolation & purification), Glutaredoxins (metabolism), Helminth Proteins (chemistry), Helminth Proteins (genetics), Helminth Proteins (isolation & purification), Helminth Proteins (metabolism), Multienzyme Complexes (chemistry), Multienzyme Complexes (genetics), Multienzyme Complexes (isolation & purification), Multienzyme Complexes (metabolism), Mutation (MeSH), NADH, NADPH Oxidoreductases (chemistry), NADH, NADPH Oxidoreductases (genetics), NADH, NADPH Oxidoreductases (isolation & purification), NADH, NADPH Oxidoreductases (metabolism), NADP (metabolism), Protein Binding (MeSH), Protein Conformation (drug effects), Protein Domains (MeSH), Protein Stability (MeSH), Protein Unfolding (drug effects), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (isolation & purification), Thioredoxins (metabolism), Tryptophan (chemistry), Urea (chemistry).
- MESH :
- chemical , chemistry : Flavin-Adenine Dinucleotide, Glutaredoxins, Helminth Proteins, Multienzyme Complexes, NADH, NADPH Oxidoreductases, Thioredoxins, Tryptophan, Urea.
- chemical , genetics : Glutaredoxins, Helminth Proteins, Multienzyme Complexes, NADH, NADPH Oxidoreductases, Thioredoxins.
- chemical , isolation & purification : Glutaredoxins, Helminth Proteins, Multienzyme Complexes, NADH, NADPH Oxidoreductases, Thioredoxins.
- chemical , metabolism : Dithionitrobenzoic Acid, Flavin-Adenine Dinucleotide, Glutaredoxins, Helminth Proteins, Multienzyme Complexes, NADH, NADPH Oxidoreductases, NADP, Thioredoxins.
- drug effects : Protein Conformation, Protein Unfolding.
- enzymology : Fasciola.
- Animals, Catalysis, Mutation, Protein Binding, Protein Domains, Protein Stability.
Abstract
Thioredoxin glutathione reductase (TGRsec) is a multi-domain flavoprotein that plays a principal role in redox homeostasis maintenance. We have previously demonstrated the role of selenocysteine in maintaining TGRsec structure-function, but the role of the glutaredoxin (Grx) domain and FAD is still unclear. In the present study, the urea-induced unfolding of recombinant Fasciola gigantica TGRsec (FgTGRsec) and its N-terminal truncated variant (ΔNTD-FgTGRsec) were examined to understand the role of the Grx domain and FAD in the stabilization of FgTGRsec and ΔNTD-FgTGRsec. Our results showed that both proteins underwent unfolding in a three state manner. First, the protein undergoes a conformational transition rendering a near-native state with no FAD bound, and then full unfolding of the apo-dimer occurs without dissociation. The Grx domain stabilized the global FgTGRsec structure and positively regulated FgTGRsec activity, and alteration in the FAD microenvironment was directly proportional to the loss of thioredoxin reductase (TrxR) and glutathione reductase activities. Based on these results, we concluded that the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis. Thus, we suggest that in platyhelminth parasites, during evolution, the Grx domain merged with the TrxR domain to confer higher catalytic activity and provide additional structural stability to the full-length TGR.
DOI: 10.1016/j.abb.2018.09.002
PubMed: 30205085
Affiliations:
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Electronic address: timir.tripathi@gmail.com.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong- 793022</wicri:regionArea><wicri:noRegion>Shillong- 793022</wicri:noRegion></affiliation></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="eISSN">1096-0384</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Catalysis (MeSH)</term><term>Dithionitrobenzoic Acid (metabolism)</term><term>Fasciola (enzymology)</term><term>Flavin-Adenine Dinucleotide (chemistry)</term><term>Flavin-Adenine Dinucleotide (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (isolation & purification)</term><term>Glutaredoxins (metabolism)</term><term>Helminth Proteins (chemistry)</term><term>Helminth Proteins (genetics)</term><term>Helminth Proteins (isolation & purification)</term><term>Helminth Proteins (metabolism)</term><term>Multienzyme Complexes (chemistry)</term><term>Multienzyme Complexes (genetics)</term><term>Multienzyme Complexes (isolation & purification)</term><term>Multienzyme Complexes (metabolism)</term><term>Mutation (MeSH)</term><term>NADH, NADPH Oxidoreductases (chemistry)</term><term>NADH, NADPH Oxidoreductases (genetics)</term><term>NADH, NADPH Oxidoreductases (isolation & purification)</term><term>NADH, NADPH Oxidoreductases (metabolism)</term><term>NADP (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (drug effects)</term><term>Protein Domains (MeSH)</term><term>Protein Stability (MeSH)</term><term>Protein Unfolding (drug effects)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (isolation & purification)</term><term>Thioredoxins (metabolism)</term><term>Tryptophan (chemistry)</term><term>Urea (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>5,5'-Dithiobis(acide 2-nitro-benzoïque) (métabolisme)</term><term>Animaux (MeSH)</term><term>Catalyse (MeSH)</term><term>Complexes multienzymatiques (composition chimique)</term><term>Complexes multienzymatiques (génétique)</term><term>Complexes multienzymatiques (isolement et purification)</term><term>Complexes multienzymatiques (métabolisme)</term><term>Conformation des protéines (effets des médicaments et des substances chimiques)</term><term>Domaines protéiques (MeSH)</term><term>Dépliement des protéines (effets des médicaments et des substances chimiques)</term><term>Fasciola (enzymologie)</term><term>Flavine adénine dinucléotide (composition chimique)</term><term>Flavine adénine dinucléotide (métabolisme)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (isolement et purification)</term><term>Glutarédoxines (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Mutation (MeSH)</term><term>NADH, NADPH oxidoreductases (composition chimique)</term><term>NADH, NADPH oxidoreductases (génétique)</term><term>NADH, NADPH oxidoreductases (isolement et purification)</term><term>NADH, NADPH oxidoreductases (métabolisme)</term><term>NADP (métabolisme)</term><term>Protéines d'helminthes (composition chimique)</term><term>Protéines d'helminthes (génétique)</term><term>Protéines d'helminthes (isolement et purification)</term><term>Protéines d'helminthes (métabolisme)</term><term>Stabilité protéique (MeSH)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (isolement et purification)</term><term>Thiorédoxines (métabolisme)</term><term>Tryptophane (composition chimique)</term><term>Urée (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Flavin-Adenine Dinucleotide</term><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Thioredoxins</term><term>Tryptophan</term><term>Urea</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dithionitrobenzoic Acid</term><term>Flavin-Adenine Dinucleotide</term><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>NADP</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexes multienzymatiques</term><term>Flavine adénine dinucléotide</term><term>Glutarédoxines</term><term>NADH, NADPH oxidoreductases</term><term>Protéines d'helminthes</term><term>Thiorédoxines</term><term>Tryptophane</term><term>Urée</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Conformation</term><term>Protein Unfolding</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Conformation des protéines</term><term>Dépliement des protéines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Fasciola</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fasciola</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexes multienzymatiques</term><term>Glutarédoxines</term><term>NADH, NADPH oxidoreductases</term><term>Protéines d'helminthes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Complexes multienzymatiques</term><term>Glutarédoxines</term><term>NADH, NADPH oxidoreductases</term><term>Protéines d'helminthes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>5,5'-Dithiobis(acide 2-nitro-benzoïque)</term><term>Complexes multienzymatiques</term><term>Flavine adénine dinucléotide</term><term>Glutarédoxines</term><term>NADH, NADPH oxidoreductases</term><term>NADP</term><term>Protéines d'helminthes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalysis</term><term>Mutation</term><term>Protein Binding</term><term>Protein Domains</term><term>Protein Stability</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Catalyse</term><term>Domaines protéiques</term><term>Liaison aux protéines</term><term>Mutation</term><term>Stabilité protéique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin glutathione reductase (TGRsec) is a multi-domain flavoprotein that plays a principal role in redox homeostasis maintenance. We have previously demonstrated the role of selenocysteine in maintaining TGRsec structure-function, but the role of the glutaredoxin (Grx) domain and FAD is still unclear. In the present study, the urea-induced unfolding of recombinant Fasciola gigantica TGRsec (FgTGRsec) and its N-terminal truncated variant (ΔNTD-FgTGRsec) were examined to understand the role of the Grx domain and FAD in the stabilization of FgTGRsec and ΔNTD-FgTGRsec. Our results showed that both proteins underwent unfolding in a three state manner. First, the protein undergoes a conformational transition rendering a near-native state with no FAD bound, and then full unfolding of the apo-dimer occurs without dissociation. The Grx domain stabilized the global FgTGRsec structure and positively regulated FgTGRsec activity, and alteration in the FAD microenvironment was directly proportional to the loss of thioredoxin reductase (TrxR) and glutathione reductase activities. Based on these results, we concluded that the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis. Thus, we suggest that in platyhelminth parasites, during evolution, the Grx domain merged with the TrxR domain to confer higher catalytic activity and provide additional structural stability to the full-length TGR.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30205085</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0384</ISSN><JournalIssue CitedMedium="Internet"><Volume>656</Volume><PubDate><Year>2018</Year><Month>10</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.</ArticleTitle><Pagination><MedlinePgn>38-45</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0003-9861(18)30507-1</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.abb.2018.09.002</ELocationID><Abstract><AbstractText>Thioredoxin glutathione reductase (TGRsec) is a multi-domain flavoprotein that plays a principal role in redox homeostasis maintenance. We have previously demonstrated the role of selenocysteine in maintaining TGRsec structure-function, but the role of the glutaredoxin (Grx) domain and FAD is still unclear. In the present study, the urea-induced unfolding of recombinant Fasciola gigantica TGRsec (FgTGRsec) and its N-terminal truncated variant (ΔNTD-FgTGRsec) were examined to understand the role of the Grx domain and FAD in the stabilization of FgTGRsec and ΔNTD-FgTGRsec. Our results showed that both proteins underwent unfolding in a three state manner. First, the protein undergoes a conformational transition rendering a near-native state with no FAD bound, and then full unfolding of the apo-dimer occurs without dissociation. The Grx domain stabilized the global FgTGRsec structure and positively regulated FgTGRsec activity, and alteration in the FAD microenvironment was directly proportional to the loss of thioredoxin reductase (TrxR) and glutathione reductase activities. Based on these results, we concluded that the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis. Thus, we suggest that in platyhelminth parasites, during evolution, the Grx domain merged with the TrxR domain to confer higher catalytic activity and provide additional structural stability to the full-length TGR.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kalita</LastName><ForeName>Parismita</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong- 793022, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shukla</LastName><ForeName>Harish</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong- 793022, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gadhave</LastName><ForeName>Kundlik</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>School of Basic Sciences, Indian Institute of Technology Mandi, Kamand, Himachal Pradesh, 175005, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Giri</LastName><ForeName>Rajanish</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>School of Basic Sciences, Indian Institute of Technology Mandi, Kamand, Himachal Pradesh, 175005, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tripathi</LastName><ForeName>Timir</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong- 793022, India. Electronic address: timir.tripathi@gmail.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>09</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015801">Helminth Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>146-14-5</RegistryNumber><NameOfSubstance UI="D005182">Flavin-Adenine Dinucleotide</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>8W8T17847W</RegistryNumber><NameOfSubstance UI="D014508">Urea</NameOfSubstance></Chemical><Chemical><RegistryNumber>9BZQ3U62JX</RegistryNumber><NameOfSubstance UI="D004228">Dithionitrobenzoic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.-</RegistryNumber><NameOfSubstance UI="D009247">NADH, NADPH Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.4.-</RegistryNumber><NameOfSubstance UI="C466433">thioredoxin glutathione reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004228" MajorTopicYN="N">Dithionitrobenzoic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005209" MajorTopicYN="N">Fasciola</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005182" MajorTopicYN="N">Flavin-Adenine Dinucleotide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015801" MajorTopicYN="N">Helminth Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="N">Multienzyme Complexes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009247" MajorTopicYN="N">NADH, NADPH Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="Y">Protein Domains</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058767" MajorTopicYN="N">Protein Unfolding</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014508" MajorTopicYN="N">Urea</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Activity</Keyword><Keyword MajorTopicYN="Y">FAD</Keyword><Keyword MajorTopicYN="Y">Fluorescence</Keyword><Keyword MajorTopicYN="Y">Glutathione reductase</Keyword><Keyword MajorTopicYN="Y">Liver fluke</Keyword><Keyword MajorTopicYN="Y">Parasite</Keyword><Keyword MajorTopicYN="Y">Stability</Keyword><Keyword MajorTopicYN="Y">Thioredoxin glutathione reductase</Keyword><Keyword MajorTopicYN="Y">Thioredoxin reductase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>06</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>09</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>09</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>9</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>9</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30205085</ArticleId><ArticleId IdType="pii">S0003-9861(18)30507-1</ArticleId><ArticleId IdType="doi">10.1016/j.abb.2018.09.002</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Kalita, Parismita" sort="Kalita, Parismita" uniqKey="Kalita P" first="Parismita" last="Kalita">Parismita Kalita</name></noRegion><name sortKey="Gadhave, Kundlik" sort="Gadhave, Kundlik" uniqKey="Gadhave K" first="Kundlik" last="Gadhave">Kundlik Gadhave</name><name sortKey="Giri, Rajanish" sort="Giri, Rajanish" uniqKey="Giri R" first="Rajanish" last="Giri">Rajanish Giri</name><name sortKey="Shukla, Harish" sort="Shukla, Harish" uniqKey="Shukla H" first="Harish" last="Shukla">Harish Shukla</name><name sortKey="Tripathi, Timir" sort="Tripathi, Timir" uniqKey="Tripathi T" first="Timir" last="Tripathi">Timir Tripathi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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