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The Interface Between the Biological and Inorganic Worlds: Iron-Sulfur Metalloclusters
Douglas C. Rees1 and
James B. Howard2
Complex iron-sulfur metalloclusters form the active sites ofthe enzymes that catalyze redox transformations of N2, CO, andH2, which are likely components of Earth's primordial atmosphere.Although these centers reflect the organizational principlesof simpler iron-sulfur clusters, they exhibit extensive elaborationsthat confer specific ligand-binding and catalytic properties.These changes were probably achieved through evolutionary processes,including the fusion of small clusters, the addition of newmetals, and the development of cluster assembly pathways, drivenby selective pressures resulting from changes in the chemicalcomposition of the biosphere.
1 Division of Chemistry and Chemical Engineering 114-96, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA. 2 Department of Biochemistry, University of Minnesota, Minneapolis, MN 55455, USA. E-mail: dcrees{at}caltech.edu (D.C.R.); howar001{at}umn.edu (J.B.H.)
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The Outer Mitochondrial Membrane Protein mitoNEET Contains a Novel Redox-active 2Fe-2S Cluster.
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Molecular Insights into Nitrogenase FeMoco Insertion: TRP-444 OF MoFe PROTEIN {alpha}-SUBUNIT LOCKS FeMoco IN ITS BINDING SITE.
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The effect of oxygen on biochemical networks and the evolution of complex life..
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Interchangeability and Distinct Properties of Bacterial Fe-S Cluster Assembly Systems: Functional Replacement of the isc and suf Operons in Escherichia coli with the nifSU-Like Operon from Helicobacter pylori.
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J. Biochem.
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Formation and characterization of an all-ferrous Rieske cluster and stabilization of the [2Fe-2S]0 core by protonation.
E. J. Leggate, E. Bill, T. Essigke, G. M. Ullmann, and J. Hirst (2004)
PNAS
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