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Iron-sulfur clusters: nature's modular, multipurpose structures.
Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.
Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity.
- N. Khoroshilova, C. Popescu, E. Münck, H. Beinert, P. Kiley
- ChemistryProceedings of the National Academy of Sciences…
- 10 June 1997
The transcription factor FNR (fumarate nitrate reduction) requires the presence of an iron-sulfur (Fe-S) cluster for its function as a global transcription regulator in Escherichia coli when oxygen…
Endonuclease III is an iron-sulfur protein.
Elemental analyses, Mössbauer, and EPR data show that endonuclease III of Escherichia coli is unique in being both a DNA repair enzyme and an iron-sulfur protein.
Recombinant toluene-4-monooxygenase: catalytic and Mössbauer studies of the purified diiron and rieske components of a four-protein complex.
A novel, four-component oxygenase combining elements from the soluble methane oxidation complex of the methanotrophic bacteria and the aromatic hydroxylation complexes of the soil pseudomonads is defined.
Characterization of the [2Fe-2S] cluster of Escherichia coli transcription factor IscR.
Characterization of anaerobically isolated IscR using resonance Raman, Mössbauer, and nuclear magnetic resonance spectroscopies leads to the proposal that the [2Fe-2S] cluster does not have full cysteinyl ligation, and Mutagenesis studies indicate that the highly conserved His107 residue is essential for cluster ligation.
Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase.
Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli.
- C. Popescu, D. Bates, H. Beinert, E. Münck, P. Kiley
- BiologyProceedings of the National Academy of Sciences…
- 10 November 1998
It is demonstrated that 57Fe Mössbauer spectroscopy can be employed to study the in vivo behavior of (overexpressed) proteins and that a significant amount of the [4Fe-4S]2+ cluster is regenerated when the cells are shifted back to an anaerobic environment.
Substitution of Leucine 28 with Histidine in theEscherichia coli Transcription Factor FNR Results in Increased Stability of the [4Fe-4S]2+ Cluster to Oxygen*
A mutant FNR protein containing a substitution of Leu-28 with His (FNR-L28H) which, unlike its wild type (WT) counterpart, is functional under aerobic growth conditions is characterized and a model to explain how WT-FNR is normally inactivated under aerobic grow conditions is presented.
Crystallographic and spectroscopic characterization of a nonheme Fe(IV)-O complex.
High-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.
Nonheme FeIVO complexes that can oxidize the C-H bonds of cyclohexane at room temperature.
Nonheme oxoiron(IV) complexes of two pentadentate ligands have been generated and found to have spectroscopic properties similar to the closely related tetradentate TPA (tris(2-pyridylmethyl)amine) complex reported earlier.