Ferredoxin (Fd) and ferredoxin-NADP(+)-reductase (FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance (NMR)-restrained-docking approach, two alternative structural models of the Fd-FNR complex in the presence of NADP+ are proposed. The protein docking simulations were performed with the software BiGGER. NMR titration revealed a 1:1 stoichiometry for the complex and allowed the mapping of the interacting residues at the surface of Fd. The NMR chemical shifts were encoded into distance constraints and used with theoretically calculated electronic coupling between the redox cofactors to propose experimentally validated docked complexes.
[NMR paper] Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by
Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range.
Related Articles Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range.
Biochim Biophys Acta. 2005 Apr-May;1707(2-3):254-8
Authors: Pedersen A, Johansson T, Rydström J, Göran Karlsson B
A pH-titration 2D NMR study of Escherichia coli transhydrogenase domain III with...
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[NMR paper] Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-eno
Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
Related Articles Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
J Biomol NMR. 2004 Jan;28(1):11-29
Authors: McDowell LM, Poliks B, Studelska DR, O'Connor RD, Beusen DD, Schaefer J
The 46-kD enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate-3-phosphate (S3P) and phosphoenolpyruvate to form EPSP....
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[NMR paper] Heteronuclear NMR and soft docking: an experimental approach for a structural model o
Heteronuclear NMR and soft docking: an experimental approach for a structural model of the cytochrome c553-ferredoxin complex.
Related Articles Heteronuclear NMR and soft docking: an experimental approach for a structural model of the cytochrome c553-ferredoxin complex.
Biochemistry. 2000 Mar 14;39(10):2530-7
Authors: Morelli X, Dolla A, Czjzek M, Palma PN, Blasco F, Krippahl L, Moura JJ, Guerlesquin F
The combination of docking algorithms with NMR data has been developed extensively for the studies of protein-ligand interactions. However, to...
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[NMR paper] NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas
NMR spectroscopic studies of the hydrogenosomal ferredoxin from Trichomonas vaginalis: hyperfine-shifted 1H resonances.
Related Articles NMR spectroscopic studies of the hydrogenosomal ferredoxin from Trichomonas vaginalis: hyperfine-shifted 1H resonances.
J Inorg Biochem. 1998 Dec;72(3-4):127-31
Authors: Liu HY, Germanas JP
The hyperfine-shifted 1H NMR resonances of oxidized and reduced Trichomonas vaginalis ferredoxin, a functionally unique ferredoxin, have been studied. The oxidized protein spectrum displayed a pattern of six broad...
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[NMR paper] NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and imped
NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two clusters.
Related Articles NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two clusters.
Biochemistry. 1995 Jan 10;34(1):194-205
Authors: Huber JG, Gaillard J, Moulis JM
The 2 ferredoxin from Chromatium vinosum has been investigated by 1H and 13C nuclear magnetic resonance. 1H NMR sequence-specific assignments have been obtained for a large majority of...
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[NMR paper] 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum.
1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum.
Related Articles 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum.
Biochem Int. 1992 Mar;26(4):577-85
Authors: Ganadu ML, Bonomi F, Pagani S, Boelens R
The 8Fe-8S ferredoxin from Clostridium pasteurianum was investigated by 1D and 2D 1H NMR. Spectra of a well-structured, full native preparation of the oxidized protein in 1 M NaCl at pH 8.0 are presented. Assignments of non-isotropically shifted resonances in the diamagnetic region of the spectrum,...
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[NMR paper] 13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the ami
13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the amines using formaldehyde.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the amines using formaldehyde.
Biochim Biophys Acta. 1990 Apr 19;1038(2):146-51
Authors: Gluck M, Sweeney WV
Clostridium pasteurianum 2(4Fe-4S) ferredoxin has been reductively methylated using formaldehyde and sodium cyanoborohydride....
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[NMR paper] Structural changes in the recombinant, NADP(H)-binding component of proton translocat
Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
FEBS Lett. 1999 Mar 5;446(1):127-32
Authors: Quirk PG, Jeeves M, Cotton NP, Smith JK, Jackson BJ
We have analysed 1H, 15N-HSQC spectra of the...
Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
Linear Mode
