Related ArticlesNMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters.
Biochemistry. 1995 Jan 10;34(1):194-205
Authors: Huber JG, Gaillard J, Moulis JM
The 2[4Fe-4S] 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 the residues. They indicate that the protein folds along a pattern similar to that previously evidenced for shorter 2[4Fe-4S] ferredoxins. However, C. vinosum ferredoxin differs from other ferredoxins by the occurrence of a turn in an eight amino acid region separating two successive cysteines, Cys-40 and Cys-49, liganding one cluster. Also, the unique C-terminal end of C. vinosum ferredoxin contains a 10 amino acid alpha-helix which interacts with one side of the above turn. The only cysteine of the sequence not involved in the ligation of the [4Fe-4S] clusters is Cys-57. Specific NMR experiments helped characterizing the signals arising from the ligands of these clusters: most of them display properties reminiscent of those of homologous ferredoxins, except for the signals associated with Cys-40. Despite the general similarity between C. vinosum ferredoxin and other 2[4Fe-4S] ferredoxins, the electron paramagnetic resonance and NMR spectra of the former reduced protein are significantly different from those previously observed for S = 1/2 [4Fe-4S]+ clusters. In addition, the intramolecular electron transfer rate in C. vinosum is far slower than in other similar cases. This is the first report of impeded electron exchange between two [4Fe-4S] clusters expected to be less than 12 A apart.
[NMR paper] Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
Related Articles Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
FEBS Lett. 2005 Aug 29;579(21):4585-90
Authors: Palma PN, Lagoutte B, Krippahl L, Moura JJ, Guerlesquin F
Ferredoxin (Fd) and ferredoxin-NADP(+)-reductase (FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance...
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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] Evidence for oxidation-state-dependent conformational changes in human ferredoxin fro
Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.
Related Articles Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy.
Biochemistry. 1998 Mar 17;37(11):3965-73
Authors: Xia B, Volkman BF, Markley JL
Human ferredoxin belongs to the vertebrate ferredoxin family which includes bovine adrenodoxin. It is a small (13.8 kDa) acidic protein with a cluster. It functions as an electron...
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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] NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural altera
NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
Eur J Biochem. 1991 Jun 1;198(2):285-91
Authors: Yamamoto Y, Chûjô R, Suzuki T...
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[NMR paper] 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nucle
1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
Related Articles 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
Biochemistry. 1990 Jun 12;29(23):5633-7
Authors: Cowan JA, Sola M
1H nuclear Overhauser effect experiments on the isotropically shifted signals of oxidized Chromatium vinosum HiPIP have been used to identify the four beta-CH2 geminal couples of the cysteine ligands. A partial assignment to...
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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] Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxi
Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2 ferredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2 ferredoxin.
Biochemistry. 1999 May 11;38(19):6335-45
Authors: Kyritsis P, Kümmerle R, Huber JG, Gaillard J, Guigliarelli B, Popescu C, Münck E, Moulis JM
The ferredoxin from Chromatium vinosum (CvFd) exhibits sequence and structure peculiarities. Its two Fe4S4(SCys)4 clusters have unusually...
NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and imped
Linear Mode
