AustralieFrV1, PascalFrancis, Curation, bibRecord, 004D54

Hydrogenases as catalysts for fuel cells: Strategies for efficient immobilization at electrode interfaces

Identifieur interne : 004D54 ( PascalFrancis/Curation ); précédent : 004D53; suivant : 004D55

Hydrogenases as catalysts for fuel cells: Strategies for efficient immobilization at electrode interfaces

Auteurs : Elisabeth Lojou [France]

Source :

Electrochimica acta [ 0013-4686 ] ; 2011.

RBID : Pascal:12-0325089

Descripteurs français

Pascal (Inist)
- Catalyse enzymatique, Origine microbienne, Enzyme immobilisée, Electrode, Bactérie, Couche monomoléculaire, Couche autoassemblée, Nanotube carbone, Liposome, Pile combustible biochimique, Article synthèse, Electrocatalyse, Hydrolases, Aquifex aeolicus.

English descriptors

KwdEn :
- Bacteria, Biochemical fuel cell, Carbon nanotubes, Electrocatalysis, Electrodes, Enzymatic catalysis, Hydrolases, Immobilized enzyme, Liposome, Microbial origin, Monolayer, Review, Self-assembled layer.

Abstract

Hydrogenases are the key enzymes for hydrogen metabolism in many microorganisms. Due to the high efficiency they develop for H₂ oxidation, research in the last five years has aimed towards their use as biocatalysts for H₂/O₂ biofuel cells to replace platinum-based chemical catalysts. We report in this review the major issues that have been addressed in view of the future development of such a novel biotechnological device. This includes enhancing the stability of either the enzyme itself or its immobilization onto conductive supports, increasing the amount of electrically connected enzymes and, finally, controlling hydrogenase orientation at the electrode surface, and hence the electron transfer process. We specifically focus on a particular [NiFe] membrane-bound hydrogenase purified from the hyperthermophilic and microaerophilic bacterium Aquifex aeolicus. This enzyme resists to O₂, CO, and high temperatures making it potentially efficient as a biocatalyst. Recent progress in these domains strengthens the credibility of a viable H₂/O₂ biofuel cell and opens new avenues for biofuel cell design.

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A08	`01`	`1`	`ENG`	`@1 Hydrogenases as catalysts for fuel cells: Strategies for efficient immobilization at electrode interfaces`
A09	`01`	`1`	`ENG`	`@1 Electrochemistry from Biology to Physics`
A11	`01`	`1`		`@1 LOJOU (Elisabeth)`
A12	`01`	`1`		`@1 BERGEL (A.) @9 ed.`
A12	`02`	`1`		`@1 BOND (A. M.) @9 ed.`
A12	`03`	`1`		`@1 BRANKOVIC (S.) @9 ed.`
A12	`04`	`1`		`@1 BULTEL (Y.) @9 ed.`
A12	`05`	`1`		`@1 DI QUARTO (F.) @9 ed.`
A12	`06`	`1`		`@1 GORTON (L.) @9 ed.`
A12	`07`	`1`		`@1 INZELT (G.) @9 ed.`
A12	`08`	`1`		`@1 LAPICQUE (F.) @9 ed.`
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A12	`10`	`1`		`@1 OPALLO (M.) @9 ed.`
A12	`11`	`1`		`@1 SAVINOVA (E. R.) @9 ed.`
A12	`12`	`1`		`@1 TOH (C.S.) @9 ed.`
A12	`13`	`1`		`@1 TSIRLINA (G. A.) @9 ed.`
A12	`14`	`1`		`@1 VIVIER (V.) @9 ed.`
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A15	`01`			`@1 CNRS @2 Toulouse @3 FRA @Z 1 aut.`
A15	`02`			`@1 Monash University @2 Clayton, Vic. @3 AUS @Z 2 aut.`
A15	`03`			`@1 University of Houston @2 Houston, TX @3 USA @Z 3 aut.`
A15	`04`			`@1 LEPMI @2 Grenoble @3 FRA @Z 4 aut.`
A15	`05`			`@1 University of Palermo @3 ITA @Z 5 aut.`
A15	`06`			`@1 Lund University @3 SWE @Z 6 aut.`
A15	`07`			`@1 Eotvos Lorand University @2 Budapest @3 HUN @Z 7 aut.`
A15	`08`			`@1 CNRS @2 Nancy @3 FRA @Z 8 aut.`
A15	`09`			`@1 Wildau University @3 DEU @Z 9 aut.`
A15	`10`			`@1 Polish Academy of Sciences @2 Warsaw @3 POL @Z 10 aut.`
A15	`11`			`@1 Université de Strasbourg @3 FRA @Z 11 aut.`
A15	`12`			`@1 Nanyang Technological University @3 SGP @Z 12 aut.`
A15	`13`			`@1 Moscow State University @3 RUS @Z 13 aut.`
A15	`14`			`@1 Université Pierre et Marie Curie @2 Paris @3 FRA @Z 14 aut.`
A15	`15`			`@1 University of Münster @3 DEU @Z 15 aut.`
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C02	`01`	`X`		`@0 001D06D03E`
C02	`02`	`X`		`@0 230`
C03	`01`	`X`	`FRE`	`@0 Catalyse enzymatique @5 02`
C03	`01`	`X`	`ENG`	`@0 Enzymatic catalysis @5 02`
C03	`01`	`X`	`SPA`	`@0 Catálisis enzimática @5 02`
C03	`02`	`X`	`FRE`	`@0 Origine microbienne @5 03`
C03	`02`	`X`	`ENG`	`@0 Microbial origin @5 03`
C03	`02`	`X`	`SPA`	`@0 Origen microbiano @5 03`
C03	`03`	`X`	`FRE`	`@0 Enzyme immobilisée @5 04`
C03	`03`	`X`	`ENG`	`@0 Immobilized enzyme @5 04`
C03	`03`	`X`	`SPA`	`@0 Enzima inmovilizada @5 04`
C03	`04`	`X`	`FRE`	`@0 Electrode @5 05`
C03	`04`	`X`	`ENG`	`@0 Electrodes @5 05`
C03	`04`	`X`	`SPA`	`@0 Electrodo @5 05`
C03	`05`	`X`	`FRE`	`@0 Bactérie @5 06`
C03	`05`	`X`	`ENG`	`@0 Bacteria @5 06`
C03	`05`	`X`	`SPA`	`@0 Bacteria @5 06`
C03	`06`	`X`	`FRE`	`@0 Couche monomoléculaire @5 07`
C03	`06`	`X`	`ENG`	`@0 Monolayer @5 07`
C03	`06`	`X`	`SPA`	`@0 Capa monomolecular @5 07`
C03	`07`	`X`	`FRE`	`@0 Couche autoassemblée @5 08`
C03	`07`	`X`	`ENG`	`@0 Self-assembled layer @5 08`
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C03	`08`	`3`	`FRE`	`@0 Nanotube carbone @5 09`
C03	`08`	`3`	`ENG`	`@0 Carbon nanotubes @5 09`
C03	`09`	`X`	`FRE`	`@0 Liposome @5 10`
C03	`09`	`X`	`ENG`	`@0 Liposome @5 10`
C03	`09`	`X`	`SPA`	`@0 Liposoma @5 10`
C03	`10`	`X`	`FRE`	`@0 Pile combustible biochimique @5 11`
C03	`10`	`X`	`ENG`	`@0 Biochemical fuel cell @5 11`
C03	`10`	`X`	`SPA`	`@0 Pila combustible bioquímica @5 11`
C03	`11`	`X`	`FRE`	`@0 Article synthèse @5 12`
C03	`11`	`X`	`ENG`	`@0 Review @5 12`
C03	`11`	`X`	`SPA`	`@0 Artículo síntesis @5 12`
C03	`12`	`X`	`FRE`	`@0 Electrocatalyse @5 13`
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C03	`13`	`X`	`FRE`	`@0 Hydrolases @2 FE @5 14`
C03	`13`	`X`	`ENG`	`@0 Hydrolases @2 FE @5 14`
C03	`13`	`X`	`SPA`	`@0 Hydrolases @2 FE @5 14`
C03	`14`	`X`	`FRE`	`@0 Aquifex aeolicus @2 NS @4 INC @5 76`
C07	`01`	`X`	`FRE`	`@0 Enzyme @2 FE`
C07	`01`	`X`	`ENG`	`@0 Enzyme @2 FE`
C07	`01`	`X`	`SPA`	`@0 Enzima @2 FE`
N21				`@1 247`

A30	`01`	`1`	`ENG`	`@1 International Society of Electrochemistry (ISE) Meeting @2 61 @3 Nice FRA @4 2010-09-26`

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Hydrogenases are the key enzymes for hydrogen metabolism in many microorganisms. Due to the high efficiency they develop for H<sub>2</sub>
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/O<sub>2</sub>
 biofuel cells to replace platinum-based chemical catalysts. We report in this review the major issues that have been addressed in view of the future development of such a novel biotechnological device. This includes enhancing the stability of either the enzyme itself or its immobilization onto conductive supports, increasing the amount of electrically connected enzymes and, finally, controlling hydrogenase orientation at the electrode surface, and hence the electron transfer process. We specifically focus on a particular [NiFe] membrane-bound hydrogenase purified from the hyperthermophilic and microaerophilic bacterium Aquifex aeolicus. This enzyme resists to O<sub>2</sub>
, CO, and high temperatures making it potentially efficient as a biocatalyst. Recent progress in these domains strengthens the credibility of a viable H<sub>2</sub>
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 biofuel cell and opens new avenues for biofuel cell design.</s0>
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<fC03 i1="02" i2="X" l="SPA"><s0>Origen microbiano</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Enzyme immobilisée</s0>
<s5>04</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Immobilized enzyme</s0>
<s5>04</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Enzima inmovilizada</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Electrode</s0>
<s5>05</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Electrodes</s0>
<s5>05</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Electrodo</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Bactérie</s0>
<s5>06</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Bacteria</s0>
<s5>06</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Bacteria</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Couche monomoléculaire</s0>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Monolayer</s0>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Capa monomolecular</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Couche autoassemblée</s0>
<s5>08</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Self-assembled layer</s0>
<s5>08</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Capa autoensamblada</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="3" l="FRE"><s0>Nanotube carbone</s0>
<s5>09</s5>
</fC03>
<fC03 i1="08" i2="3" l="ENG"><s0>Carbon nanotubes</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Liposome</s0>
<s5>10</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Liposome</s0>
<s5>10</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Liposoma</s0>
<s5>10</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Pile combustible biochimique</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Biochemical fuel cell</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Pila combustible bioquímica</s0>
<s5>11</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Article synthèse</s0>
<s5>12</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Review</s0>
<s5>12</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Artículo síntesis</s0>
<s5>12</s5>
</fC03>
<fC03 i1="12" i2="X" l="FRE"><s0>Electrocatalyse</s0>
<s5>13</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Electrocatalysis</s0>
<s5>13</s5>
</fC03>
<fC03 i1="12" i2="X" l="SPA"><s0>Electrocatálisis</s0>
<s5>13</s5>
</fC03>
<fC03 i1="13" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
<s5>14</s5>
</fC03>
<fC03 i1="13" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
<s5>14</s5>
</fC03>
<fC03 i1="13" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
<s5>14</s5>
</fC03>
<fC03 i1="14" i2="X" l="FRE"><s0>Aquifex aeolicus</s0>
<s2>NS</s2>
<s4>INC</s4>
<s5>76</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fN21><s1>247</s1>
</fN21>
</pA>
<pR><fA30 i1="01" i2="1" l="ENG"><s1>International Society of Electrochemistry (ISE) Meeting</s1>
<s2>61</s2>
<s3>Nice FRA</s3>
<s4>2010-09-26</s4>
</fA30>
</pR>
</standard>
</inist>
</record>

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	Serveur d'exploration sur les relations entre la France et l'Australie
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Hydrogenases as catalysts for fuel cells: Strategies for efficient immobilization at electrode interfaces

Hydrogenases as catalysts for fuel cells: Strategies for efficient immobilization at electrode interfaces

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