Title : Effective immobilization of alcohol dehydrogenase on carbon nanoscaffolds for ethanol biofuel cell.

Pub. Date : 2017 Dec

PMID : 28772201






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The ADH entrapped within the MADQUAT that was present on the carbon nanoscaffolds exhibited a high electron exchange capability with the electrode through its cofactor beta-nicotinamide adenine dinucleotide hydrate and beta-nicotinamide adenine dinucleotide reduced disodium salt hydrate (NAD+/NADH) redox reaction. NAD aldo-keto reductase family 1 member A1 Homo sapiens
2 The ADH entrapped within the MADQUAT that was present on the carbon nanoscaffolds exhibited a high electron exchange capability with the electrode through its cofactor beta-nicotinamide adenine dinucleotide hydrate and beta-nicotinamide adenine dinucleotide reduced disodium salt hydrate (NAD+/NADH) redox reaction. NAD aldo-keto reductase family 1 member A1 Homo sapiens
3 The ADH entrapped within the MADQUAT that was present on the carbon nanoscaffolds exhibited a high electron exchange capability with the electrode through its cofactor beta-nicotinamide adenine dinucleotide hydrate and beta-nicotinamide adenine dinucleotide reduced disodium salt hydrate (NAD+/NADH) redox reaction. NAD aldo-keto reductase family 1 member A1 Homo sapiens