Photosensitized H2 generation from "one-pot" and "two-pot" assemblies of a zinc-porphyrin/platinum nanoparticle/protein scaffold.
Identifieur interne : 001367 ( PubMed/Curation ); précédent : 001366; suivant : 001368Photosensitized H2 generation from "one-pot" and "two-pot" assemblies of a zinc-porphyrin/platinum nanoparticle/protein scaffold.
Auteurs : Emily R. Clark [États-Unis] ; Donald M. Kurtz [États-Unis]Source :
- Dalton transactions (Cambridge, England : 2003) [ 1477-9234 ] ; 2016.
Descripteurs français
- KwdFr :
- Cytochromes de type b (), Cytochromes de type b (génétique), Cytochromes de type b (métabolisme), Escherichia coli (métabolisme), Ferritines (), Ferritines (génétique), Ferritines (métabolisme), Hydrogène (), Lumière, Métalloporphyrines (), Nanoparticules métalliques (), Oxydoréduction, Photosensibilisants (), Photosensibilisants (métabolisme), Platine (), Protéines bactériennes (), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines recombinantes (), Protéines recombinantes (biosynthèse), Protéines recombinantes (isolement et purification).
- MESH :
- biosynthèse : Protéines recombinantes.
- génétique : Cytochromes de type b, Ferritines, Protéines bactériennes.
- isolement et purification : Protéines recombinantes.
- métabolisme : Cytochromes de type b, Escherichia coli, Ferritines, Photosensibilisants, Protéines bactériennes.
- Cytochromes de type b, Ferritines, Hydrogène, Lumière, Métalloporphyrines, Nanoparticules métalliques, Oxydoréduction, Photosensibilisants, Platine, Protéines bactériennes, Protéines recombinantes.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Cytochrome b Group (chemistry), Cytochrome b Group (genetics), Cytochrome b Group (metabolism), Escherichia coli (metabolism), Ferritins (chemistry), Ferritins (genetics), Ferritins (metabolism), Hydrogen (chemistry), Light, Metal Nanoparticles (chemistry), Metalloporphyrins (chemistry), Oxidation-Reduction, Photosensitizing Agents (chemistry), Photosensitizing Agents (metabolism), Platinum (chemistry), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification).
- MESH :
- chemical , biosynthesis : Recombinant Proteins.
- chemical , chemistry : Bacterial Proteins, Cytochrome b Group, Ferritins, Hydrogen, Metalloporphyrins, Photosensitizing Agents, Platinum, Recombinant Proteins.
- chemical , genetics : Bacterial Proteins, Cytochrome b Group, Ferritins.
- chemical , isolation & purification : Recombinant Proteins.
- chemical , metabolism : Bacterial Proteins, Cytochrome b Group, Ferritins, Photosensitizing Agents.
- chemistry : Metal Nanoparticles.
- metabolism : Escherichia coli.
- Light, Oxidation-Reduction.
Abstract
We report photosensitized H2 generation using a protein scaffold that nucleates formation of platinum nanoparticles (Pt NPs) and contains "built-in" photosensitizers. The photosensitizers, zinc-protoporphyrin IX or zinc-mesoporphyrin IX (ZnP) were incorporated in place of the naturally occurring heme in the 24-subunit iron storage protein bacterioferritin (Bfr) when the ZnPs were added to the E. coli expression medium. We engineered a stable dimeric Bfr variant with two protein subunits sandwiching a ZnP. Ten glycines were also substituted in place of residues surrounding the vinyl side of the porphyrin in order increase access of solvent and/or redox agents. An optimized "one-pot" reaction of this glycine-substituted ZnMP-Bfr dimer with a Pt(iv) salt and borohydride resulted in a ∼50 : 50 mixture of protein in the form of Pt-free glycine-substituted ZnP-Bfr dimers and re-assembled 24-mers surrounding Pt NPs formed in situ. H2 production occurred upon visible light irradiation of this "one-pot" product when combined with triethanolamine as sacrificial electron donor and methyl viologen as electron relay. An analogous "two-pot" system containing mixtures of separately prepared Pt-free glycine-substituted ZnP-Bfr dimer and porphyrin-free Pt NP@Bfr 24-mer also showed robust photosensitized H2 generation. The glycine-substituted-ZnP-Bfr dimer thus served as photosensitizer for catalytic reduction of methyl viologen by triethanolamine, and the reduced methyl viologen was able to transfer electrons across the Bfr 24-mer protein shell to generate H2 at the enclosed Pt NP in a "dark" reaction. Our results demonstrate that Bfr is a readily manipulatable and versatile scaffold for photosensitized redox chemistry.
DOI: 10.1039/c5dt03418c
PubMed: 26616549
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Clark</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, USA. donald.kurtz@utsa.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, University of Texas at San Antonio, San Antonio, TX</wicri:regionArea></affiliation></author><author><name sortKey="Kurtz, Donald M" sort="Kurtz, Donald M" uniqKey="Kurtz D" first="Donald M" last="Kurtz">Donald M. Kurtz</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, USA. donald.kurtz@utsa.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, University of Texas at San Antonio, San Antonio, TX</wicri:regionArea></affiliation></author></analytic><series><title level="j">Dalton transactions (Cambridge, England : 2003)</title><idno type="eISSN">1477-9234</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (genetics)</term><term>Bacterial Proteins (metabolism)</term><term>Cytochrome b Group (chemistry)</term><term>Cytochrome b Group (genetics)</term><term>Cytochrome b Group (metabolism)</term><term>Escherichia coli (metabolism)</term><term>Ferritins (chemistry)</term><term>Ferritins (genetics)</term><term>Ferritins (metabolism)</term><term>Hydrogen (chemistry)</term><term>Light</term><term>Metal Nanoparticles (chemistry)</term><term>Metalloporphyrins (chemistry)</term><term>Oxidation-Reduction</term><term>Photosensitizing Agents (chemistry)</term><term>Photosensitizing Agents (metabolism)</term><term>Platinum (chemistry)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (isolation & purification)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cytochromes de type b ()</term><term>Cytochromes de type b (génétique)</term><term>Cytochromes de type b (métabolisme)</term><term>Escherichia coli (métabolisme)</term><term>Ferritines ()</term><term>Ferritines (génétique)</term><term>Ferritines (métabolisme)</term><term>Hydrogène ()</term><term>Lumière</term><term>Métalloporphyrines ()</term><term>Nanoparticules métalliques ()</term><term>Oxydoréduction</term><term>Photosensibilisants ()</term><term>Photosensibilisants (métabolisme)</term><term>Platine ()</term><term>Protéines bactériennes ()</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (isolement et purification)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Cytochrome b Group</term><term>Ferritins</term><term>Hydrogen</term><term>Metalloporphyrins</term><term>Photosensitizing Agents</term><term>Platinum</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Cytochrome b Group</term><term>Ferritins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Cytochrome b Group</term><term>Ferritins</term><term>Photosensitizing Agents</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Metal Nanoparticles</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytochromes de type b</term><term>Ferritines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytochromes de type b</term><term>Escherichia coli</term><term>Ferritines</term><term>Photosensibilisants</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Light</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cytochromes de type b</term><term>Ferritines</term><term>Hydrogène</term><term>Lumière</term><term>Métalloporphyrines</term><term>Nanoparticules métalliques</term><term>Oxydoréduction</term><term>Photosensibilisants</term><term>Platine</term><term>Protéines bactériennes</term><term>Protéines recombinantes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report photosensitized H2 generation using a protein scaffold that nucleates formation of platinum nanoparticles (Pt NPs) and contains "built-in" photosensitizers. The photosensitizers, zinc-protoporphyrin IX or zinc-mesoporphyrin IX (ZnP) were incorporated in place of the naturally occurring heme in the 24-subunit iron storage protein bacterioferritin (Bfr) when the ZnPs were added to the E. coli expression medium. We engineered a stable dimeric Bfr variant with two protein subunits sandwiching a ZnP. Ten glycines were also substituted in place of residues surrounding the vinyl side of the porphyrin in order increase access of solvent and/or redox agents. An optimized "one-pot" reaction of this glycine-substituted ZnMP-Bfr dimer with a Pt(iv) salt and borohydride resulted in a ∼50 : 50 mixture of protein in the form of Pt-free glycine-substituted ZnP-Bfr dimers and re-assembled 24-mers surrounding Pt NPs formed in situ. H2 production occurred upon visible light irradiation of this "one-pot" product when combined with triethanolamine as sacrificial electron donor and methyl viologen as electron relay. An analogous "two-pot" system containing mixtures of separately prepared Pt-free glycine-substituted ZnP-Bfr dimer and porphyrin-free Pt NP@Bfr 24-mer also showed robust photosensitized H2 generation. The glycine-substituted-ZnP-Bfr dimer thus served as photosensitizer for catalytic reduction of methyl viologen by triethanolamine, and the reduced methyl viologen was able to transfer electrons across the Bfr 24-mer protein shell to generate H2 at the enclosed Pt NP in a "dark" reaction. Our results demonstrate that Bfr is a readily manipulatable and versatile scaffold for photosensitized redox chemistry. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26616549</PMID><DateCompleted><Year>2016</Year><Month>09</Month><Day>28</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1477-9234</ISSN><JournalIssue CitedMedium="Internet"><Volume>45</Volume><Issue>2</Issue><PubDate><Year>2016</Year><Month>Jan</Month><Day>14</Day></PubDate></JournalIssue><Title>Dalton transactions (Cambridge, England : 2003)</Title><ISOAbbreviation>Dalton Trans</ISOAbbreviation></Journal><ArticleTitle>Photosensitized H2 generation from "one-pot" and "two-pot" assemblies of a zinc-porphyrin/platinum nanoparticle/protein scaffold.</ArticleTitle><Pagination><MedlinePgn>630-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c5dt03418c</ELocationID><Abstract><AbstractText>We report photosensitized H2 generation using a protein scaffold that nucleates formation of platinum nanoparticles (Pt NPs) and contains "built-in" photosensitizers. The photosensitizers, zinc-protoporphyrin IX or zinc-mesoporphyrin IX (ZnP) were incorporated in place of the naturally occurring heme in the 24-subunit iron storage protein bacterioferritin (Bfr) when the ZnPs were added to the E. coli expression medium. We engineered a stable dimeric Bfr variant with two protein subunits sandwiching a ZnP. Ten glycines were also substituted in place of residues surrounding the vinyl side of the porphyrin in order increase access of solvent and/or redox agents. An optimized "one-pot" reaction of this glycine-substituted ZnMP-Bfr dimer with a Pt(iv) salt and borohydride resulted in a ∼50 : 50 mixture of protein in the form of Pt-free glycine-substituted ZnP-Bfr dimers and re-assembled 24-mers surrounding Pt NPs formed in situ. H2 production occurred upon visible light irradiation of this "one-pot" product when combined with triethanolamine as sacrificial electron donor and methyl viologen as electron relay. An analogous "two-pot" system containing mixtures of separately prepared Pt-free glycine-substituted ZnP-Bfr dimer and porphyrin-free Pt NP@Bfr 24-mer also showed robust photosensitized H2 generation. The glycine-substituted-ZnP-Bfr dimer thus served as photosensitizer for catalytic reduction of methyl viologen by triethanolamine, and the reduced methyl viologen was able to transfer electrons across the Bfr 24-mer protein shell to generate H2 at the enclosed Pt NP in a "dark" reaction. Our results demonstrate that Bfr is a readily manipulatable and versatile scaffold for photosensitized redox chemistry. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Clark</LastName><ForeName>Emily R</ForeName><Initials>ER</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, USA. donald.kurtz@utsa.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kurtz</LastName><ForeName>Donald M</ForeName><Initials>DM</Initials><Suffix>Jr</Suffix><AffiliationInfo><Affiliation>Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, USA. donald.kurtz@utsa.edu.</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Dalton Trans</MedlineTA><NlmUniqueID>101176026</NlmUniqueID><ISSNLinking>1477-9226</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003573">Cytochrome b Group</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008665">Metalloporphyrins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017319">Photosensitizing Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>49DFR088MY</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Cytochrome b Group</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005293" MajorTopicYN="N">Ferritins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006859" MajorTopicYN="N">Hydrogen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008027" MajorTopicYN="N">Light</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053768" MajorTopicYN="N">Metal Nanoparticles</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008665" MajorTopicYN="N">Metalloporphyrins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017319" MajorTopicYN="N">Photosensitizing Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010984" MajorTopicYN="N">Platinum</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>12</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>9</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26616549</ArticleId><ArticleId IdType="doi">10.1039/c5dt03418c</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix 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