caa a22 4500 477135811 CHVBK 20180405111717.0 cr unu---uuuuu 170330e19970701xx s 000 0 eng 10.1023/A:1018380509735 doi (NATIONALLICENCE)springer-10.1023/A:1018380509735 Backbone dynamics of oxidized and reduced D. vulgaris flavodoxin in solution [Elektronische Daten] [Andrea Hrovat, Markus Blümel, Frank Löhr, Stephen Mayhew, and Rüterjans] Recombinant Desulfovibrio vulgaris flavodoxin was produced inEscherichia coli. A complete backbone NMR assignment for the two-electronreduced protein revealed significant changes of chemical shift valuescompared to the oxidized protein, in particular for the flavinemononucleotide (FMN)-binding site. A comparison of homo- and heteronuclearNOESY spectra for the two redox states led to the assumption that reductionis not accompanied by significant changes of the global fold of the protein.The backbone dynamics of both the oxidized and reduced forms of D. vulgarisflavodoxin were investigated using two-dimensional15N-1H correlation NMR spectroscopy.T1, T2 and NOE data are obtained for 95%of the backbone amide groups in both redox states. These values wereanalysed in terms of the 'model-free‘ approach introduced by Lipari andSzabo [(1982) J. Am. Chem. Soc., 104, 4546-;4559, 4559-;4570]. Acomparison of the two redox states indicates that in the reduced speciessignificantly more flexibility occurs in the two loop regions enclosing FMN.Also, a higher amplitude of local motion could be found for the N(3)H groupof FMN bound to the reduced protein compared to the oxidized state. Kluwer Academic Publishers, 1997 Flavodoxin nationallicence Protein dynamics nationallicence Order parameter nationallicence 15N relaxation nationallicence Hrovat Andrea Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut Blümel Markus Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut Löhr Frank Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut Mayhew Stephen Department of Biochemistry, University College Dublin, Dublin 4, Belfield, Ireland aut Rüterjans and Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut Journal of Biomolecular NMR Kluwer Academic Publishers 10/1(1997-07-01), 53-62 0925-2738 10:1<53 1997 10 10858 https://doi.org/10.1023/A:1018380509735 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018380509735 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hrovat Andrea Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Blümel Markus Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Löhr Frank Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Mayhew Stephen Department of Biochemistry, University College Dublin, Dublin 4, Belfield, Ireland aut NATIONALLICENCE 700 1- Rüterjans and Institute of Biophysical Chemistry, Marie Curie Strasse 9, D-60439, Frankfurt, Germany aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 10/1(1997-07-01), 53-62 0925-2738 10:1<53 1997 10 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer