Thermodynamics of binding of the distal calcium to manganese peroxidase.
Identifieur interne : 000B94 ( Main/Exploration ); précédent : 000B93; suivant : 000B95Thermodynamics of binding of the distal calcium to manganese peroxidase.
Auteurs : G R Sutherland [États-Unis] ; S D AustSource :
- Biochemistry [ 0006-2960 ] ; 1997.
Descripteurs français
- KwdFr :
- Anilino-naphtalènesulfonates (métabolisme), Basidiomycota (enzymologie), Calcium (métabolisme), Calcium (pharmacologie), Calorimétrie (MeSH), Cinétique (MeSH), Colorants fluorescents (métabolisme), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (MeSH), Liaison aux protéines (MeSH), Peroxidases (composition chimique), Peroxidases (métabolisme), Sites de fixation (MeSH), Spectrophotométrie (MeSH), Stabilité enzymatique (MeSH), Température (MeSH), Thermodynamique (MeSH).
- MESH :
- composition chimique : Peroxidases.
- enzymologie : Basidiomycota.
- métabolisme : Anilino-naphtalènesulfonates, Calcium, Colorants fluorescents, Peroxidases.
- pharmacologie : Calcium.
- Calorimétrie, Cinétique, Concentration en ions d'hydrogène, Conformation des protéines, Liaison aux protéines, Sites de fixation, Spectrophotométrie, Stabilité enzymatique, Température, Thermodynamique.
English descriptors
- KwdEn :
- Anilino Naphthalenesulfonates (metabolism), Basidiomycota (enzymology), Binding Sites (MeSH), Calcium (metabolism), Calcium (pharmacology), Calorimetry (MeSH), Enzyme Stability (MeSH), Fluorescent Dyes (metabolism), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Peroxidases (chemistry), Peroxidases (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Spectrophotometry (MeSH), Temperature (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Peroxidases.
- chemical , metabolism : Anilino Naphthalenesulfonates, Calcium, Fluorescent Dyes, Peroxidases.
- enzymology : Basidiomycota.
- chemical , pharmacology : Calcium.
- Binding Sites, Calorimetry, Enzyme Stability, Hydrogen-Ion Concentration, Kinetics, Protein Binding, Protein Conformation, Spectrophotometry, Temperature, Thermodynamics.
Abstract
We previously demonstrated that manganese peroxidase from Phanerochaete chrysosporiumwas susceptible to thermal inactivation due to release of the distal calcium, which maintained the distal heme environment of the enzyme [Sutherland, G. R. J., Zapanta, L. S., Tien, M., & Aust, S. D. (1997) Biochemistry 36, 3654-3662]. In this investigation the binding of calcium to the distal calcium binding site of manganese peroxidase was studied by optical absorption spectroscopy and isothermal titration calorimetry. The dissociation constant for the distal calcium binding site was 11 +/- 1 microM and the Hill coefficient was 1.1 +/- 0.1. The binding of calcium was accompanied by decreases in enthalpy and entropy that were large compared to those of other calcium binding proteins. The decreases were consistent with the large conformational changes proposed to occur in manganese peroxidase as a result of the binding and release of the distal calcium. Studies involving binding of the hydrophobic fluorescent probe, 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid, dipotassium salt (bis-ANS), to manganese peroxidase indicated that the active, calcium-containing form of the enzyme had less exposed hydrophobic surface area, which would contribute to an increase in enthalpy and entropy upon calcium binding. Therefore, the negative changes in enthalpy and entropy associated with calcium binding were attributed to a large increase in the structural rigidity and compactness of the enzyme. The dissociation constant for calcium decreased and the rate of thermal inactivation decreased with decreasing pH. However, both the ability of calcium to prevent thermal inactivation of manganese peroxidase and the rate of calcium binding decreased as the pH decreased. Therefore it was proposed that, at lower pH, calcium binding to manganese peroxidase was more thermodynamically favorable, but the rate of calcium binding decreased because the flexibility of the calcium binding site, and in turn exposure of the ligands to the incoming ion, decreased.
DOI: 10.1021/bi970484k
PubMed: 9214302
Affiliations:
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sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anilino Naphthalenesulfonates (metabolism)</term><term>Basidiomycota (enzymology)</term><term>Binding Sites (MeSH)</term><term>Calcium (metabolism)</term><term>Calcium (pharmacology)</term><term>Calorimetry (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Fluorescent Dyes (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Kinetics (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Spectrophotometry (MeSH)</term><term>Temperature (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anilino-naphtalènesulfonates (métabolisme)</term><term>Basidiomycota (enzymologie)</term><term>Calcium (métabolisme)</term><term>Calcium (pharmacologie)</term><term>Calorimétrie (MeSH)</term><term>Cinétique (MeSH)</term><term>Colorants fluorescents (métabolisme)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Spectrophotométrie (MeSH)</term><term>Stabilité enzymatique (MeSH)</term><term>Température (MeSH)</term><term>Thermodynamique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anilino Naphthalenesulfonates</term><term>Calcium</term><term>Fluorescent Dyes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Anilino-naphtalènesulfonates</term><term>Calcium</term><term>Colorants fluorescents</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Calcium</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Calcium</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Calorimetry</term><term>Enzyme Stability</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Protein Binding</term><term>Protein Conformation</term><term>Spectrophotometry</term><term>Temperature</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Calorimétrie</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Liaison aux protéines</term><term>Sites de fixation</term><term>Spectrophotométrie</term><term>Stabilité enzymatique</term><term>Température</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We previously demonstrated that manganese peroxidase from Phanerochaete chrysosporiumwas susceptible to thermal inactivation due to release of the distal calcium, which maintained the distal heme environment of the enzyme [Sutherland, G. R. J., Zapanta, L. S., Tien, M., & Aust, S. D. (1997) Biochemistry 36, 3654-3662]. In this investigation the binding of calcium to the distal calcium binding site of manganese peroxidase was studied by optical absorption spectroscopy and isothermal titration calorimetry. The dissociation constant for the distal calcium binding site was 11 +/- 1 microM and the Hill coefficient was 1.1 +/- 0.1. The binding of calcium was accompanied by decreases in enthalpy and entropy that were large compared to those of other calcium binding proteins. The decreases were consistent with the large conformational changes proposed to occur in manganese peroxidase as a result of the binding and release of the distal calcium. Studies involving binding of the hydrophobic fluorescent probe, 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid, dipotassium salt (bis-ANS), to manganese peroxidase indicated that the active, calcium-containing form of the enzyme had less exposed hydrophobic surface area, which would contribute to an increase in enthalpy and entropy upon calcium binding. Therefore, the negative changes in enthalpy and entropy associated with calcium binding were attributed to a large increase in the structural rigidity and compactness of the enzyme. The dissociation constant for calcium decreased and the rate of thermal inactivation decreased with decreasing pH. However, both the ability of calcium to prevent thermal inactivation of manganese peroxidase and the rate of calcium binding decreased as the pH decreased. Therefore it was proposed that, at lower pH, calcium binding to manganese peroxidase was more thermodynamically favorable, but the rate of calcium binding decreased because the flexibility of the calcium binding site, and in turn exposure of the ligands to the incoming ion, decreased.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9214302</PMID><DateCompleted><Year>1997</Year><Month>08</Month><Day>15</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>36</Volume><Issue>28</Issue><PubDate><Year>1997</Year><Month>Jul</Month><Day>15</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Thermodynamics of binding of the distal calcium to manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>8567-73</MedlinePgn></Pagination><Abstract><AbstractText>We previously demonstrated that manganese peroxidase from Phanerochaete chrysosporiumwas susceptible to thermal inactivation due to release of the distal calcium, which maintained the distal heme environment of the enzyme [Sutherland, G. R. J., Zapanta, L. S., Tien, M., & Aust, S. D. (1997) Biochemistry 36, 3654-3662]. In this investigation the binding of calcium to the distal calcium binding site of manganese peroxidase was studied by optical absorption spectroscopy and isothermal titration calorimetry. The dissociation constant for the distal calcium binding site was 11 +/- 1 microM and the Hill coefficient was 1.1 +/- 0.1. The binding of calcium was accompanied by decreases in enthalpy and entropy that were large compared to those of other calcium binding proteins. The decreases were consistent with the large conformational changes proposed to occur in manganese peroxidase as a result of the binding and release of the distal calcium. Studies involving binding of the hydrophobic fluorescent probe, 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid, dipotassium salt (bis-ANS), to manganese peroxidase indicated that the active, calcium-containing form of the enzyme had less exposed hydrophobic surface area, which would contribute to an increase in enthalpy and entropy upon calcium binding. Therefore, the negative changes in enthalpy and entropy associated with calcium binding were attributed to a large increase in the structural rigidity and compactness of the enzyme. The dissociation constant for calcium decreased and the rate of thermal inactivation decreased with decreasing pH. However, both the ability of calcium to prevent thermal inactivation of manganese peroxidase and the rate of calcium binding decreased as the pH decreased. Therefore it was proposed that, at lower pH, calcium binding to manganese peroxidase was more thermodynamically favorable, but the rate of calcium binding decreased because the flexibility of the calcium binding site, and in turn exposure of the ligands to the incoming ion, decreased.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sutherland</LastName><ForeName>G R</ForeName><Initials>GR</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan, Utah 84322-4705, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000817">Anilino Naphthalenesulfonates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005456">Fluorescent Dyes</NameOfSubstance></Chemical><Chemical><RegistryNumber>63741-13-9</RegistryNumber><NameOfSubstance UI="C035763">5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000817" MajorTopicYN="N">Anilino Naphthalenesulfonates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002151" MajorTopicYN="N">Calorimetry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005456" MajorTopicYN="N">Fluorescent Dyes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>7</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>7</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>7</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9214302</ArticleId><ArticleId IdType="doi">10.1021/bi970484k</ArticleId><ArticleId IdType="pii">bi970484k</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Sutherland, G R" sort="Sutherland, G R" uniqKey="Sutherland G" first="G R" last="Sutherland">G R Sutherland</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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