Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mössbauer and EPR spectroscopy
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Frank Neese | Eckhard Bill | Wolfgang Lubitz | Dmytro Bykov | F. Neese | W. Lubitz | Róbert Izsák | E. Bill | M. Giudici-Orticoni | P. Infossi | Maria-Eirini Pandelia | Robert Izsak | Pascale Infossi | Marie-Thérèse Giudici-Orticoni | M. Pandelia | D. Bykov
[1] V. Schünemann,et al. Structure and dynamics of biomolecules studied by Mössbauer spectroscopy , 2000 .
[2] R. Hedderich,et al. The CCG-domain-containing subunit SdhE of succinate:quinone oxidoreductase from Sulfolobus solfataricus P2 binds a [4Fe–4S] cluster , 2008, JBIC Journal of Biological Inorganic Chemistry.
[3] R. Cammack,et al. Electron-spin-resonance/electron-paramagnetic-resonance spectroscopy of iron-sulphur enzymes. , 1985, Biochemical Society transactions.
[4] H. Beinert. Iron-sulfur proteins: ancient structures, still full of surprises , 2000, JBIC Journal of Biological Inorganic Chemistry.
[5] E. Duin,et al. Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mössbauer and multifrequency EPR study. , 1994, Biochemistry.
[6] J. W. Peters,et al. Redox-dependent structural changes in the nitrogenase P-cluster. , 1997, Biochemistry.
[7] J. Gaillard,et al. Characterization of [4Fe-4Se]2+/3+ high-potential iron−sulfur protein from Chromatium vinosum , 1988 .
[8] H. Heering,et al. Reversible super-reduction of the cubane [4Fe-4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions. EPR spectroscopic and electrochemical studies. , 1995, European journal of biochemistry.
[9] S. Ciurli,et al. Subsite-differentiated analogs of native iron sulfide [4Fe-4S]2+ clusters: preparation of clusters with five- and six-coordinate subsites and modulation of redox potentials and charge distributions , 1990 .
[10] K. Yoon,et al. Purification and characterization of a highly thermostable, oxygen-resistant, respiratory [NiFe]-hydrogenase from a marine, aerobic hydrogen-oxidizing bacterium Hydrogenovibrio marinus , 2011 .
[11] A. Volbeda,et al. X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli , 2012, Proceedings of the National Academy of Sciences.
[12] Michel Frey,et al. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas , 1995, Nature.
[13] H. Heering,et al. Reversible super-reduction of the cubane [4Fe-4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions: EPR spectroscopic and electrochemical studies. , 1995 .
[14] B. Guigliarelli,et al. Study of the spin-spin interactions between the metal centers of Desulfovibrio gigas aldehyde oxidoreductase: identification of the reducible sites of the [2Fe-2S]1+,2+ clusters. , 2005, Biochemistry.
[15] M. Teixeira,et al. On the active sites of the [NiFe] hydrogenase from Desulfovibrio gigas. Mössbauer and redox-titration studies. , 1987, The Journal of biological chemistry.
[16] T. Ichiye,et al. Cleavage of [4Fe-4S]-type clusters: breaking the symmetry. , 2009, The journal of physical chemistry. A.
[17] G. Schneider,et al. Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. , 1997, Structure.
[18] J. Mouesca,et al. Iron–sulfur clusters and their electronic and magnetic properties , 1998 .
[19] J. Berg,et al. Principles Of Bioinorganic Chemistry , 1994 .
[20] M. Teixeira,et al. Redox intermediates of Desulfovibrio gigas [NiFe] hydrogenase generated under hydrogen. Mössbauer and EPR characterization of the metal centers. , 1989, The Journal of biological chemistry.
[21] F. Armstrong,et al. A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. , 2011, Nature chemical biology.
[22] B. Fox,et al. Mössbauer and EPR studies of the photoactivation of nitrile hydratase. , 2001, Biochemistry.
[23] C. Spahn,et al. The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre , 2011, Nature.
[24] P. Schürmann,et al. Role of histidine-86 in the catalytic mechanism of ferredoxin:thioredoxin reductase. , 2009, Biochemistry.
[25] M. Rohmer,et al. Isoprenoid biosynthesis via the MEP pathway: in vivo Mössbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein. , 2009, Journal of the American Chemical Society.
[26] Edward I. Solomon,et al. Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin , 2007, Science.
[27] F. Armstrong,et al. Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. , 2011, Journal of the American Chemical Society.
[28] W. Lubitz,et al. Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus , 2011, Proceedings of the National Academy of Sciences.
[29] A. Dey,et al. Mixed Valent Sites in Biological Electron Transfer , 2008 .
[30] D. Kurtz. Oxo- and hydroxo-bridged diiron complexes: a chemical perspective on a biological unit , 1990 .
[31] W. Lubitz,et al. Evolution and diversification of Group 1 [NiFe] hydrogenases. Is there a phylogenetic marker for O(2)-tolerance? , 2012, Biochimica et biophysica acta.
[32] Philip Hinchliffe,et al. Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus , 2006, Science.
[33] H. Beinert,et al. Iron-sulfur clusters: nature's modular, multipurpose structures. , 1997, Science.
[34] D. Case,et al. Spin Densities and Spin Coupling in Iron-Sulfur Clusters: A New Analysis of Hyperfine Coupling Constants , 1995 .
[35] E. Münck,et al. Iron-sulfur proteins: spin-coupling model for three-iron clusters. , 1980, Proceedings of the National Academy of Sciences of the United States of America.
[36] Y. Higuchi,et al. Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase , 2011, Nature.
[37] J. Rush,et al. Interpretation of the Mössbauer spectra of the high-potential iron protein from Chromatium. , 1980, European journal of biochemistry.
[38] C. Krebs,et al. Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study. , 2002, Journal of the American Chemical Society.
[39] D. Case,et al. Orbital interactions, electron delocalization and spin coupling in iron-sulfur clusters , 1995 .