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  Rational redesign of the ferredoxin-NADP+-oxido-reductase/ferredoxin-interaction for photosynthesis-dependent H2-production

Wiegand, K., Winkler, M., Rumpel, S., Kannchen, D., Rexroth, S., Hase, T., et al. (2018). Rational redesign of the ferredoxin-NADP+-oxido-reductase/ferredoxin-interaction for photosynthesis-dependent H2-production. Biochimica et Biophysica Acta, Bioenergetics, 1859(4), 253-262. doi:10.1016/j.bbabio.2018.01.006.

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 Creators:
Wiegand, K.1, Author
Winkler, M.2, Author
Rumpel, S.3, Author
Kannchen, D.1, Author
Rexroth, S.1, Author
Hase, T.4, Author
Farès, C.5, Author              
Happe, T.2, Author
Lubitz, W.3, Author
Rögner, M.1, Author
Affiliations:
1Plant Biochemistry, Faculty of Biology & Biotechnology, Ruhr University Bochum, 44780 Bochum, Germany, ou_persistent22              
2Photobiotechnology, Faculty of Biology & Biotechnology, Ruhr University Bochum, 44780 Bochum, Germany, ou_persistent22              
3Max-Planck-Institut für Chemische Energiekonversion, 45470 Mülheim, Germany, ou_persistent22              
4Institute for Protein Research, Osaka University, Suita 565-0871, Osaka, Japan, ou_persistent22              
5Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445623              

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Free keywords: Protein design; Protein interaction; FNR; NMR; Photosynthesis; Synechocystis
 Abstract: Utilization of electrons from the photosynthetic water splitting reaction for the generation of biofuels, commodities as well as application in biotransformations requires a partial rerouting of the photosynthetic electron transport chain. Due to its rather negative redox potential and its bifurcational function, ferredoxin at the acceptor side of Photosystem 1 is one of the focal points for such an engineering. With hydrogen production as model system, we show here the impact and potential of redox partner design involving ferredoxin (Fd), ferredoxin-oxido-reductase (FNR) and [FeFe]‑hydrogenase HydA1 on electron transport in a future cyanobacterial design cell of Synechocystis PCC 6803. X-ray-structure-based rational design and the allocation of specific interaction residues by NMR-analysis led to the construction of Fd- and FNR-mutants, which in appropriate combination enabled an about 18-fold enhanced electron flow from Fd to HydA1 (in competition with equimolar amounts of FNR) in in vitro assays. The negative impact of these mutations on the Fd-FNR electron transport which indirectly facilitates H2 production (with a contribution of ≤42% by FNR variants and ≤23% by Fd-variants) and the direct positive impact on the Fd-HydA1 electron transport (≤23% by Fd-mutants) provide an excellent basis for the construction of a hydrogen-producing design cell and the study of photosynthetic efficiency-optimization with cyanobacteria.

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Language(s): eng - English
 Dates: 2017-09-052018-01-222018-01-312018-04-01
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbabio.2018.01.006
 Degree: -

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1859 (4) Sequence Number: - Start / End Page: 253 - 262 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6