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Coenzyme Engineering of a Hyperthermophilic 6-Phosphogluconate Dehydrogenase from NADP(+) to NAD(+) with Its Application to Biobatteries

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dc.contributor.authorChen, Huien
dc.contributor.authorZhu, Zhiguangen
dc.contributor.authorHuang, Ruien
dc.contributor.authorZhang, Y. H. Percivalen
dc.contributor.departmentBiological Systems Engineeringen
dc.date.accessioned2017-01-18T03:10:18Zen
dc.date.available2017-01-18T03:10:18Zen
dc.date.issued2016-11-02en
dc.description.abstractEngineering the coenzyme specificity of redox enzymes plays an important role in metabolic engineering, synthetic biology, and biocatalysis, but it has rarely been applied to bioelectrochemistry. Here we develop a rational design strategy to change the coenzyme specificity of 6-phosphogluconate dehydrogenase (6PGDH) from a hyperthermophilic bacterium Thermotoga maritima from its natural coenzyme NADP(+) to NAD(+). Through amino acid-sequence alignment of NADP(+)-and NAD(+)-preferred 6PGDH enzymes and computer-aided substrate-coenzyme docking, the key amino acid residues responsible for binding the phosphate group of NADP(+) were identified. Four mutants were obtained via site-directed mutagenesis. The best mutant N32E/R33I/T34I exhibited a x 6.4 x 10(4)-fold reversal of the coenzyme selectivity from NADP(+) to NAD(+). The maximum power density and current density of the biobattery catalyzed by the mutant were 0.135 mW cm(-2) and 0.255 mA cm(-2), similar to 25% higher than those obtained from the wide-type 6PGDH-based biobattery at the room temperature. By using this 6PGDH mutant, the optimal temperature of running the biobattery was as high as 65 degrees C, leading to a high power density of 1.75 mW cm(-2). This study demonstrates coenzyme engineering of a hyperthermophilic 6PGDH and its application to high-temperature biobatteries.en
dc.description.notesThis project cannot be carried out without support of the Biological System Engineering Department, Virginia Polytechnic Institute and State University, Virginia. It was mainly funded by DOE EERE award (DE-EE0006968) and partially supported by the Virginia Agricultural Experiment Station and the Hatch Program of the National Institute of Food and Agriculture, U.S. Department of Agriculture.en
dc.description.sponsorshipBiological System Engineering Department, Virginia Polytechnic Institute and State University, Virginia; DOE EERE award [DE-EE0006968]; Virginia Agricultural Experiment Station; Hatch Program of the National Institute of Food and Agriculture, U.S. Department of Agricultureen
dc.description.versionPublished versionen
dc.format.extent? - ? (8) page(s)en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1038/srep36311en
dc.identifier.issn2045-2322en
dc.identifier.pmid27805055en
dc.identifier.urihttp://hdl.handle.net/10919/74379en
dc.identifier.volume6en
dc.language.isoenen
dc.publisherNature Publishing Groupen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000387250000001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectketol-acid reductoisomeraseen
dc.subjectenzymatic biofuel cellsen
dc.subjectalcohol-dehydrogenaseen
dc.subjectescherichia-colien
dc.subjectcofactoren
dc.subjectspecificityen
dc.subjectglucoseen
dc.subjectdesignen
dc.subjectnadhen
dc.subjectbiocatalysisen
dc.titleCoenzyme Engineering of a Hyperthermophilic 6-Phosphogluconate Dehydrogenase from NADP(+) to NAD(+) with Its Application to Biobatteriesen
dc.title.serialScientific Reportsen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biological Systems Engineeringen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen

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