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  • Land, HenrikUppsala universitet,Molekylär biomimetik (författare)

Discovery of novel [FeFe]-hydrogenases for biocatalytic H-2-production

  • Artikel/kapitelEngelska2019

Förlag, utgivningsår, omfång ...

  • 2019
  • Royal Society of Chemistry (RSC),2019
  • electronicrdacarrier

Nummerbeteckningar

  • LIBRIS-ID:oai:DiVA.org:uu-397949
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-397949URI
  • https://doi.org/10.1039/c9sc03717aDOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:ref swepub-contenttype
  • Ämneskategori:art swepub-publicationtype

Anmärkningar

  • A new screening method for [FeFe]-hydrogenases is described, circumventing the need for specialized expression conditions as well as protein purification for initial characterization. [FeFe]-hydrogenases catalyze the formation and oxidation of molecular hydrogen at rates exceeding 10(3) s(-1), making them highly promising for biotechnological applications. However, the discovery of novel [FeFe]-hydrogenases is slow due to their oxygen sensitivity and dependency on a structurally unique cofactor, complicating protein expression and purification. Consequently, only a very limited number have been characterized, hampering their implementation. With the purpose of increasing the throughput of [FeFe]-hydrogenase discovery, we have developed a screening method that allows for rapid identification of novel [FeFe]-hydrogenases as well as their characterization with regards to activity (activity assays and protein film electrochemistry) and spectroscopic properties (electron paramagnetic resonance and Fourier transform infrared spectroscopy). The method is based on in vivo artificial maturation of [FeFe]-hydrogenases in Escherichia coli and all procedures are performed on either whole cells or non-purified cell lysates, thereby circumventing extensive protein purification. The screening was applied on eight putative [FeFe]-hydrogenases originating from different structural sub-classes and resulted in the discovery of two new active [FeFe]-hydrogenases. The [FeFe]-hydrogenase from Solobacterium moorei shows high H-2-gas production activity, while the enzyme from Thermoanaerobacter mathranii represents a hitherto uncharacterized [FeFe]-hydrogenase sub-class. This latter enzyme is a putative sensory hydrogenase and our in vivo spectroscopy study reveals distinct differences compared to the well established H-2 producing HydA1 hydrogenase from Chlamydomonas reinhardtii.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Ceccaldi, PierreUppsala universitet,Molekylär biomimetik(Swepub:uu)piece309 (författare)
  • Meszaros, Livia S.Uppsala universitet,Molekylär biomimetik(Swepub:uu)livme315 (författare)
  • Lorenzi, MarcoUppsala universitet,Molekylär biomimetik(Swepub:uu)marlo670 (författare)
  • Redman, Holly J.Uppsala universitet,Molekylär biomimetik(Swepub:uu)holre224 (författare)
  • Senger, MoritzFree Univ Berlin, Inst Expt Phys, Expt Mol Biophys, Arnimallee 14, DE-14195 Berlin, Germany (författare)
  • Stripp, Sven T.Free Univ Berlin, Inst Expt Phys, Expt Mol Biophys, Arnimallee 14, DE-14195 Berlin, Germany (författare)
  • Berggren, GustavUppsala universitet,Molekylär biomimetik(Swepub:uu)guber255 (författare)
  • Uppsala universitetMolekylär biomimetik (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Chemical Science: Royal Society of Chemistry (RSC)10:43, s. 9941-99482041-65202041-6539

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