Ferritin encapsulation of artificial metalloenzymes: engineering a tertiary coordination sphere for an artificial transfer hydrogenase

dc.accessRightsAnonymous
dc.audienceScience
dc.contributor.authorHestericová, Martina
dc.contributor.authorHeinisch, Tillmann
dc.contributor.authorLenz, Markus
dc.contributor.authorWard, Thomas R.
dc.date.accessioned2018-12-13T09:50:37Z
dc.date.available2018-12-13T09:50:37Z
dc.date.issued2018-07
dc.description.abstractFerritin, a naturally occuring iron-storage protein, plays an important role in nanoengineering and biomedical applications. Upon iron removal, apoferritin was shown to allow the encapsulation of an artificial transfer hydrogenase (ATHase) based on the streptavidin-biotin technology. The third coordination sphere, provided by ferritin, significantly influences the catalytic activity of an ATHase for the reduction of cyclic imines.
dc.identifier.doi10.1039/C8DT02224K
dc.identifier.issn1477-9234
dc.identifier.issn1477-9226
dc.identifier.urihttp://hdl.handle.net/11654/26944
dc.issue32
dc.language.isoenen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.ispartofDalton Transactionsen_US
dc.subjectferritin
dc.subjectapoferritin
dc.subjectartificial transfer hydrogenase (ATHase)
dc.subjectstreptavidin-biotin technology
dc.titleFerritin encapsulation of artificial metalloenzymes: engineering a tertiary coordination sphere for an artificial transfer hydrogenase
dc.type01A - Beitrag in wissenschaftlicher Zeitschrift
dc.volume47
dspace.entity.typePublication
fhnw.InventedHereYes
fhnw.IsStudentsWorkno
fhnw.PublishedSwitzerlandNo
fhnw.ReviewTypeAnonymous ex ante peer review of a complete publication
fhnw.affiliation.hochschuleHochschule für Life Sciences FHNWde_CH
fhnw.affiliation.institutInstitut für Ecopreneurshipde_CH
fhnw.pagination10837-10841
fhnw.publicationOnlineJa
fhnw.publicationStatePublished
relation.isAuthorOfPublicationc7b0a617-ef2c-48b2-919e-18d2c62cc929
relation.isAuthorOfPublication.latestForDiscoveryc7b0a617-ef2c-48b2-919e-18d2c62cc929
Dateien