Enzymatic biofuel cells utilizing a biomimetic cofactor.
The performance of immobilized enzyme systems is often limited by cofactor diffusion and regeneration. Here, we demonstrate an engineered enzyme capable of utilizing the minimal cofactor nicotinamide mononucleotide (NMN(+)) to address these limitations. Significant gains in performance are observed with NMN(+) in immobilized systems, despite a decreased turnover rate with the minimal cofactor.
Department of Chemical Engineering, Columbia University in the City of New York, New York, NY 10027, USA.
Elliot
E
Campbell
Matthew
M
Meredith
Shelley D
SD
Minteer
Scott
S
Banta
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001674:Bioelectric Energy Sources; D040761:Biomimetic Materials / Q000378:metabolism*; D003067:Coenzymes / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D009537:Nicotinamide Mononucleotide / Q000378:metabolism*; D011487:Protein Conformation; D015202:Protein Engineering; D020027:Pyrococcus furiosus / Q000201:enzymology; D013379:Substrate Specificity
D003067:Coenzymes; D004800:Enzymes, Immobilized; D009537:Nicotinamide Mononucleotide; D000426:Alcohol Dehydrogenase