Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution.

[1]  J. Gaillard,et al.  On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe-4S] ferredoxin. , 1994, Protein engineering.

[2]  I. Rayment,et al.  Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata. , 1994, Biochemistry.

[3]  A. Scozzafava,et al.  Selective interaction of ferricyanide with cluster I of Clostridium pasteurianum 2[Fe4S4] ferredoxin , 1993, FEBS letters.

[4]  J. Gaillard,et al.  Effect of replacing conserved proline residues on the EPR and NMR properties of Clostridium pasteurianum 2[4Fe-4S] ferredoxin. , 1993, Biochemistry.

[5]  J. Ulrich,et al.  Sequences of clostridial ferredoxins: determination of the Clostridium sticklandii sequence and correction of the Clostridium acidurici sequence. , 1993, The Biochemical journal.

[6]  J. Thornton,et al.  PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .

[7]  G. Tollin,et al.  Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex. , 1993, Biochemistry.

[8]  V S Lamzin,et al.  Automated refinement of protein models. , 1993, Acta crystallographica. Section D, Biological crystallography.

[9]  J. Tainer,et al.  Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III. , 1992, Science.

[10]  D. Rees,et al.  Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. , 1992, Science.

[11]  A. Scozzafava,et al.  1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianum. , 1992, European journal of biochemistry.

[12]  R. Cammack Iron−sulfur clusters in enzymes: themes and variations , 1992 .

[13]  P. Stephens,et al.  Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I. Changes in [4Fe-4S] cluster reduction potential and reactivity. , 1991, The Journal of biological chemistry.

[14]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[15]  C. Kissinger,et al.  Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 A. , 1991, Journal of molecular biology.

[16]  J. Sanders-Loehr,et al.  The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy , 1991 .

[17]  E. Smith,et al.  Redox properties of several bacterial ferredoxins using square wave voltammetry. , 1990, The Journal of biological chemistry.

[18]  H. Beinert Recent developments in the field of iron‐sulfur proteins , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[19]  C. Stout,et al.  Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[20]  T. Tsukihara,et al.  Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins. , 1989, Journal of molecular biology.

[21]  P. Stephens,et al.  Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement , 1989 .

[22]  C. Stout,et al.  Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 A resolution. , 1989, Journal of molecular biology.

[23]  W. Hendrickson,et al.  Crystal structure of Clostridium acidi-urici ferredoxin at 5-A resolution based on measurements of anomalous X-ray scattering at multiple wavelengths. , 1988, The Journal of biological chemistry.

[24]  Wolfgang Kabsch,et al.  Evaluation of Single-Crystal X-ray Diffraction Data from a Position-Sensitive Detector , 1988 .

[25]  P. Fitzgerald MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement , 1988 .

[26]  J. Pflugrath,et al.  Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography , 1987 .

[27]  J. Gaillard,et al.  Hydrogen-1 nuclear magnetic resonance of selenium-substituted clostridial ferredoxins , 1987 .

[28]  D. J. Steenkamp,et al.  Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution. , 1986, The Journal of biological chemistry.

[29]  L. K. Hanson,et al.  Redox pathways in electron-transfer proteins: correlations between reactivities, solvent exposure, and unpaired-spin-density distributions. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[30]  J. Gaillard,et al.  High-multiplicity spin states of 2[4Fe-4Se]+ clostridial ferredoxins. , 1986, Biochemistry.

[31]  C. Stout,et al.  Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues. , 1983, The Journal of biological chemistry.

[32]  L. H. Jensen,et al.  Structure of Peptococcus aerogenes ferredoxin. Refinement at 2 A resolution. , 1976, The Journal of biological chemistry.

[33]  M. Perutz,et al.  Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2 , 1975, Nature.

[34]  J. Rabinowitz,et al.  Synthesis and properties of Clostridium acidi-urici (Leu2)-ferredoxin: a function of the peptide chain and evidence against the direct role of the aromatic residues in electron transfer. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[35]  L. Sieker,et al.  Structure of a bacterial ferredoxin. , 1973, The Journal of biological chemistry.

[36]  G. Nakos,et al.  CHAPTER 2 – Bacterial Ferredoxins and/or Iron–Sulfur Proteins as Electron Carriers , 1973 .

[37]  Rall Sc,et al.  The amino acid sequence of ferredoxin from Clostridium acidi-urici. , 1969 .