dc.date.accessioned | 2019-12-09T20:51:52Z | |
dc.date.available | 2019-12-09T20:51:52Z | |
dc.date.created | 2018-08-25T07:16:26Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Gudim, Ingvild Hammerstad, Marta Lofstad, Marie Hersleth, Hans-Petter . Characterization of different flavodoxin reductase-flavodoxin (FNR-Fld) interactions reveals an efficient FNR-Fld redox pair and identifies a novel FNR subclass. Biochemistry. 2018, 57(37), 5427-5436 | |
dc.identifier.uri | http://hdl.handle.net/10852/71494 | |
dc.description.abstract | Flavodoxins (Flds) are small, bacterial proteins that transfer electrons to various redox enzymes. Flavodoxins are reduced by ferredoxin/flavodoxin NADP+ oxidoreductases (FNRs), but little is known of the FNR-Fld interaction. Here, we compare the interactions of two flavodoxins (Fld1–2), one flavodoxin-like protein (NrdI), and three different thioredoxin reductase (TrxR)-like FNRs (FNR1–3), all from Bacillus cereus. Steady-state kinetics shows that the FNR2-Fld2 electron transfer pair is particularly efficient, and redox potential measurements also indicate that this is the most favorable electron donor/acceptor pair. Furthermore, crystal structures of FNR1 and FNR2 show that the proteins have crystallized in different conformations, a closed and an open conformation, respectively. We suggest that a large-scale conformational rearrangement takes place during the FNR catalytic cycle to allow for the binding and reduction of the Fld and, subsequently, the re-reduction of the FNR by NADPH. Finally, inspection of the residues surrounding the FAD cofactor in the FNR active site shows that a key isoalloxazine ring-stacking residue is different in FNR1 and FNR2, which could explain the large difference in catalytic efficiency between the two FNRs. To date, all of the characterized TrxR-like FNRs have a residue with aromatic character stacking against the FAD isoalloxazine ring, and this has been thought to be a conserved feature of this class of FNRs. FNR1, however, has a valine in this position. Bioinformatic analysis shows that the TrxR-like FNRs can actually be divided into two groups, one group where the FAD-stacking residue has aromatic character and another group where it is valine. | en_US |
dc.language | EN | |
dc.title | Characterization of different flavodoxin reductase-flavodoxin (FNR-Fld) interactions reveals an efficient FNR-Fld redox pair and identifies a novel FNR subclass | en_US |
dc.type | Journal article | en_US |
dc.creator.author | Gudim, Ingvild | |
dc.creator.author | Hammerstad, Marta | |
dc.creator.author | Lofstad, Marie | |
dc.creator.author | Hersleth, Hans-Petter | |
cristin.unitcode | 185,15,29,40 | |
cristin.unitname | Seksjon for biokjemi og molekylærbiologi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |
dc.identifier.cristin | 1604485 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochemistry&rft.volume=57&rft.spage=5427&rft.date=2018 | |
dc.identifier.jtitle | Biochemistry | |
dc.identifier.volume | 57 | |
dc.identifier.issue | 37 | |
dc.identifier.startpage | 5427 | |
dc.identifier.endpage | 5436 | |
dc.identifier.doi | https://doi.org/10.1021/acs.biochem.8b00674 | |
dc.identifier.urn | URN:NBN:no-74602 | |
dc.subject.nvi | VDP::Kjemi: 440 | |
dc.type.document | Tidsskriftartikkel | en_US |
dc.type.peerreviewed | Peer reviewed | |
dc.source.issn | 1520-4995 | |
dc.identifier.fulltext | Fulltext https://www.duo.uio.no/bitstream/handle/10852/71494/2/Gudim-et-al-Biochem-2018.pdf | |
dc.type.version | PublishedVersion | |
dc.relation.project | NFR/231669 | |