Bioelectrocatalysis of NAD+ reduction

Cantet, Jean; Bergel, Alain; Comtat, Maurice

doi:10.1016/0302-4598(92)87021-l

Cited by 19 publications

(6 citation statements)

References 14 publications

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“…NAD(H)‐linked bidirectional hydrogenases are of particular interest for biotechnological applications as they are suited for light driven hydrogen production in vivo [73] and the regeneration of reduced purine nucleotides in biocatalytic processes [74–79]. Such applications are particularly promising as some of these enzymes are oxygen tolerant [38,58,80–82], in contrast to most other hydrogenases.…”

Section: Bidirectional Hydrogenases: Versatile Players In Biological mentioning

confidence: 99%

“…Its tolerance towards oxygen renders the SH an outstanding biocatalyst for potential biotechnological applications, in particular, since this enzyme preferentially catalyzes the production of NADH rather than its oxidation. Therefore, the SH is particularly suited for the in situ regeneration of NADH in coupled enzymatic reactions [74,76–79]. Moreover, this enzyme has been extensively studied for more than three decades and, as a consequence, it represents the best characterized bidirectional hydrogenase and an established model system for this type of enzymes.…”

Section: The Soluble Hydrogenase From Ralstonia Eutropha: a Unique Oxmentioning

confidence: 99%

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NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

et al. 2011

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a b s t r a c tHydrogenases catalyze the activation or production of molecular hydrogen. Due to their potential importance for future biotechnological applications, these enzymes have been in the focus of intense research for the past decades. Bidirectional [NiFe] hydrogenases are of particular interest as they couple the reversible cleavage of hydrogen to the redox conversion of NAD(H). In this account, we review the current state of knowledge about mechanistic aspects and structural determinants of these complex multi-cofactor enzymes. Special emphasis is laid on the oxygen-tolerant NAD(H)-linked bidirectional [NiFe] hydrogenase from Ralstonia eutropha.

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Section: Bidirectional Hydrogenases: Versatile Players In Biological mentioning

confidence: 99%

Section: The Soluble Hydrogenase From Ralstonia Eutropha: a Unique Oxmentioning

confidence: 99%

NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

et al. 2011

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“…Suspensions used for fluorescence microscopy were not passed through a 1 μm filter to allow for larger, easier-to-view vesicles. We tested for NADH enzymatic activity with lactate dehydrogenase (Sigma-Aldrich) using pyruvate as a substrate. ,, NADH was not consumed unless both enzyme and pyruvate were present.…”

Section: Methodsmentioning

confidence: 99%

Vesicle Encapsulation of a Nonbiological Photochemical System Capable of Reducing NAD⁺ to NADH

Summers

Rodoni

2015

Langmuir

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One of the fundamental structures of a cell is the membrane. Self-assembling lipid bilayer vesicles can form the membrane of an artificial cell and could also have plausibly assembled prebiotically for the origin of life. Such cell-like structures, that encapsulate some basic subset of the functions of living cells, are important for research to infer the minimum chemistry necessary for a cell, to help understand the origin of life, and to allow the production of useful species in microscopic containers. We show that the encapsulation of TiO2 particles has the potential to provide the basis for an energy transduction system inside vesicles which can be used to drive subsequent chemistry. TiO2 encapsulated in vesicles can be used to produce biochemical species such as NADH. The NADH is formed from NAD(+) reduction and is produced in a form that is able to drive further enzymatic chemistry. This allows us to link a mineral-based, nonbiological photosystem to biochemical reactions. This is a fundamental step toward being able to use this mineral photosystem in a protocell/artificial cell.

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“…The small quantity of NADH should ensure more reproducible results [41,42]. The same experiment was then carried out with a 268 lm TSEC containing 5 mM NAD þ , 0.4 mM NADH, and 20 U/ml hydrogenase.…”

Section: Hydrogenase and 316l Stainless Steelmentioning

confidence: 99%

Electron transfer between hydrogenase and 316L stainless steel: identification of a hydrogenase-catalyzed cathodic reaction in anaerobic mic

Silva

Basseguy

Bergel

2004

Journal of Electroanalytical Chemistry

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Bioelectrocatalysis of NAD+ reduction

Cited by 19 publications

References 14 publications

NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

Vesicle Encapsulation of a Nonbiological Photochemical System Capable of Reducing NAD⁺ to NADH

Electron transfer between hydrogenase and 316L stainless steel: identification of a hydrogenase-catalyzed cathodic reaction in anaerobic mic

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Bioelectrocatalysis of NAD+ reduction

Cited by 19 publications

References 14 publications

NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

Vesicle Encapsulation of a Nonbiological Photochemical System Capable of Reducing NAD+ to NADH

Electron transfer between hydrogenase and 316L stainless steel: identification of a hydrogenase-catalyzed cathodic reaction in anaerobic mic

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Vesicle Encapsulation of a Nonbiological Photochemical System Capable of Reducing NAD⁺ to NADH