Iron-sulfur clusters: nature's modular, multipurpose structures.

Iron-sulfur proteins are found in all life forms. Most frequently, they contain Fe2S2, Fe3S4, and Fe4S4 clusters. These modular clusters undergo oxidation-reduction reactions, may be inserted or removed from proteins, can influence protein structure by preferential side chain ligation, and can be interconverted. In addition to their electron transfer function, iron-sulfur clusters act as catalytic centers and sensors of iron and oxygen. Their most common oxidation states are paramagnetic and present significant challenges for understanding the magnetic properties of mixed valence systems. Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.

[1]  P. Kiley,et al.  Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[2]  J. W. Peters,et al.  Redox-dependent structural changes in the nitrogenase P-cluster. , 1997, Biochemistry.

[3]  A. L. Lacey,et al.  Structure of the [Nife] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands , 1996 .

[4]  Helmut Beinert,et al.  ACONITASE AS IRON-SULFUR PROTEIN, ENZYME, AND IRON-REGULATORY PROTEIN , 1996 .

[5]  Manoj Kumar,et al.  Nickel-Containing Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase†,‡ , 1996 .

[6]  Edward I. Solomon,et al.  Structural and Functional Aspects of Metal Sites in Biology. , 1996, Chemical reviews.

[7]  T. Oshima,et al.  Redox-linked Ionization of Sulredoxin, an Archaeal Rieske-type [2Fe-2S] Protein from Sulfolobus sp. Strain 7* , 1996, The Journal of Biological Chemistry.

[8]  B. Weiss,et al.  SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[9]  F. Armstrong,et al.  Novel Redox Chemistry of [3Fe−4S] Clusters: Electrochemical Characterization of the All-Fe(II) Form of the [3Fe−4S] Cluster Generated Reversibly in Various Proteins and Its Spectroscopic Investigation in Sulfolobus acidocaldarius Ferredoxin , 1996 .

[10]  P. Schürmann,et al.  The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters. , 1996, Biochemistry.

[11]  Edward I. Solomon,et al.  Excited-State Contributions to Ground-State Properties of Mixed-Valence Dimers: Spectral and Electronic-Structural Studies of [Fe2(OH)3(tmtacn)2]2+ Related to the [Fe2S2]+ Active Sites of Plant-Type Ferredoxins , 1996 .

[12]  M. Hentze,et al.  Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[13]  J. Meyer,et al.  Cysteine ligand swapping on a deletable loop of the [2Fe-2S] ferredoxin from Clostridium pasteurianum. , 1996, Biochemistry.

[14]  D. Coucouvanis,et al.  Catalytic Reduction of Hydrazine to Ammonia with MoFe(3)S(4)-Polycarboxylate Clusters. Possible Relevance Regarding the Function of the Molybdenum-Coordinated Homocitrate in Nitrogenase. , 1996, Inorganic chemistry.

[15]  P. Kiley,et al.  Redox control of gene expression involving iron‐sulfur proteins. Change of oxidation‐state or assembly/disassembly of Fe‐S clusters? , 1996, FEBS letters.

[16]  R. H. Holm,et al.  The Cuboidal Fe3S4 Cluster: Synthesis, Stability, and Geometric and Electronic Structures in a Non-Protein Environment , 1996 .

[17]  P. Kiley,et al.  DNA Binding and Dimerization of the Fe−S-containing FNR Protein from Escherichia coli Are Regulated by Oxygen (*) , 1996, The Journal of Biological Chemistry.

[18]  A. Lindahl,et al.  Nature of the C-Cluster in Ni-Containing Carbon Monoxide Dehydrogenases , 1996 .

[19]  M. J. Ryle,et al.  Circular Dichroism and X-ray Spectroscopies of Azotobacter vinelandii Nitrogenase Iron Protein , 1996, The Journal of Biological Chemistry.

[20]  E. Getzoff,et al.  Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions , 1995, Science.

[21]  M. Adams,et al.  Electronic, Magnetic, Redox, and Ligand-Binding Properties of [MFe3S4] Clusters (M = Zn, Co, Mn) in Pyrococcus furiosus Ferredoxin , 1995 .

[22]  T. M. Bradley,et al.  Binuclear [2Fe-2S] Clusters in the Escherichia coli SoxR Protein and Role of the Metal Centers in Transcription (*) , 1995, The Journal of Biological Chemistry.

[23]  J. Tainer,et al.  Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. , 1995, The EMBO journal.

[24]  E. L. Bominaar,et al.  Double Exchange and Vibronic Coupling in Mixed-Valence Systems. Electronic Structure of Exchange-Coupled Siroheme-[Fe4S4]2+ Chromophore in Oxidized E. Coli Sulfite Reductase , 1995 .

[25]  Michel Frey,et al.  Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas , 1995, Nature.

[26]  H. Dailey,et al.  Human ferrochelatase is an iron-sulfur protein. , 1994, Biochemistry.

[27]  I. Bertini,et al.  The electronic structure of [Fe4S4]3+ clusters in proteins. An investigation of the oxidized high-potential iron-sulfur protein II from Ectothiorhodospira vacuolata. , 1993, Biochemistry.

[28]  G. Rius,et al.  Single-crystal proton ENDOR studies of the [Fe4S4]3+ cluster: determination of the spin population distribution and proposal of a model to interpret the 1H NMR paramagnetic shifts in high-potential ferredoxins , 1993 .

[29]  D. Rees,et al.  The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. , 1993, Science.

[30]  R. Klausner,et al.  Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[31]  F. Armstrong,et al.  Investigation of metal ion uptake reactivities of [3Fe-4S] clusters in proteins : voltammetry of co-adsorbed ferredoxin-aminocyclitol films at graphite electrodes and spectroscopic identification of transformed clusters , 1991 .

[32]  D. Coucouvanis.  Use of preassembled iron/sulfur and iron/molybdenum/sulfur clusters in the stepwise synthesis of potential analogs for the Fe/Mo/S site in nitrogenase , 1991 .

[33]  Louis Noodleman,et al.  Magnetic studies of the high-potential protein model [Fe4S4(S-2,4,6-(iso-Pr)3C6H2)4]- in the [Fe4S4]3+ oxidized state , 1990 .

[34]  J. H. Miller,et al.  MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III , 1990, Nucleic Acids Res..

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

[36]  H. Zalkin,et al.  Evidence that the iron-sulfur cluster of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase determines stability of the enzyme to degradation in vivo. , 1989, The Journal of biological chemistry.

[37]  J. Moura,et al.  Moessbauer study of D. gigas ferredoxin II and spin-coupling model for Fe3S4 cluster with valence delocalization , 1987 .

[38]  H. Beinert,et al.  Mössbauer studies of aconitase. Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters. , 1985, The Journal of biological chemistry.

[39]  H. Beinert,et al.  Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase. , 1984, The Journal of biological chemistry.

[40]  J. Salerno,et al.  Exchange coupling between siroheme and iron-sulfur ([4Fe-4S]) cluster in E. coli sulfite reductase. Moessbauer studies and coupling models for a 2-electron reduced enzyme state and complexes with sulfide , 1984 .

[41]  G. L. Anderson,et al.  Reactions with the oxidized iron protein of Azotobacter vinelandii nitrogenase: formation of a 2Fe center. , 1984, Biochemistry.

[42]  Evert Jan Baerends,et al.  Electronic structure, magnetic properties, ESR, and optical spectra for 2-iron ferredoxin models by LCAO-X.alpha. valence bond theory , 1984 .

[43]  H. Beinert,et al.  Incorporation of [35S]sulfide into the Fe-S cluster of aconitase. , 1984, The Journal of biological chemistry.

[44]  J. Girerd.  Electron transfer between magnetic ions in mixed valence binuclear systems , 1983 .

[45]  K. Hagen,et al.  Synthetic routes to iron sulfide (Fe2S2, Fe3S4, Fe4S4, and Fe6S9), clusters from the common precursor tetrakis(ethanethiolate)ferrate(2-) ion ([Fe(SC2H5)4]2-): structures and properties of [Fe3S4(SR)4]3- and bis(ethanethiolate)nonathioxohexaferrate(4-) ion ([Fe6S9(SC2H5)2]4-), examples of the newest , 1983 .

[46]  J. Lipscomb,et al.  Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mössbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II. , 1982, The Journal of biological chemistry.

[47]  H. Beinert,et al.  Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[48]  J. Reynolds,et al.  Definition of reaction sequences resulting in self-assembly of [Fe4S4(SR)4]2- clusters from simple reactants , 1981 .

[49]  J. Reynolds,et al.  Core chalcogenide atom substitution reactions of [Fe2X2(SR)4]2- and [Fe4X4(SR)4]2-,3- clusters (X = sulfur, selenium) , 1981 .

[50]  W. Orme-Johnson,et al.  [29] Identification of iron-sulfur clusters in proteins , 1978 .

[51]  J. S. Chen,et al.  Quantitative extrusions of the iron sulfide(Fe4S4*) cores of the active sites of ferredoxins and the hydrogenase of Clostridium pasteurianum , 1977 .

[52]  R. Sands,et al.  Spectroscopic studies on two-iron ferredoxins , 1974, Quarterly Reviews of Biophysics.

[53]  R. Valentine,et al.  An electron transport factor from Clostridium pasteurianum. , 1962, Biochemical and biophysical research communications.

[54]  D. Arnon,et al.  Triphosphopyridine Nucleotide as a Catalyst of Photosynthetic Phosphorylation , 1957, Nature.

[55]  Clarence Zener,et al.  Interaction between the d -Shells in the Transition Metals. II. Ferromagnetic Compounds of Manganese with Perovskite Structure , 1951 .