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Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.
A reaction scheme in which the ligated solvent acts as a proton acceptor in the first half-reaction [formation of Fe(II) and oxygen] is consistent with the pH dependence of the kinetic parameters and spectroscopic properties of Fe superoxide dismutase. Expand
Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds.
Transient-state kinetic studies reveal that, upon reaction of ligninase with H2O2, spectral changes occur in the Soret region, which, by analogy to previous studies of horseradish peroxidase, are consistent with formation of Compounds I and II. Expand
Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus.
Examination of beta-galactosidase activity coded from a chromosomal phi(sodA'-'lacZ) fusion suggests that metallated Fur protein acts as a transcriptional repressor of sodA (manganese superoxide dismutase [MnSOD]; high-affinity binding of pure, Mn2(+)-Fur protein to DNA fragments containing the sodA promoter strongly suggest that sodA is part of the iron uptake regulon. Expand
The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
Comparison of available subunit I sequences reveals that the only structural elements conserved within the oxygen reductase families that could perform these functions are active-site components, namely the covalently linked histidine-tyrosine, the CuB and its ligands, and the active- site heme and itsligands. Expand
Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function
  • J. Fee
  • Biology, Medicine
  • Molecular microbiology
  • 1 November 1991
A rudimentary gene regulation model is presented which rationalizes past observations, is experimentally testable, and should serve as a guide to future research in this area. Expand
High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison.
The structure of the soluble Rieske protein from Thermus thermophilus has been determined at a resolution of 1.3 A at pH 8.5 using multiwavelength anomalous dispersion (MAD) techniques, providing evidence for a stable, oxidized cluster with a His(-) ligand and lends support to a previously proposed mechanism of coupled proton and electron transfer. Expand
Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state.
Voltammetry measurements between pH 3 and 14 reveal that all the Rieske proteins, including BphF, have pH-dependent reduction potentials with remarkably similar overall profiles, implications for the mechanism of quinol oxidation at the Q(O) site of the cytochrome bc(1) and b(6)f complexes are discussed. Expand
Integrity of thermus thermophilus cytochrome c552 Synthesized by escherichia coli cells expressing the host‐specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural
The design of Escherichia coli cells that synthesize a structurally perfect, recombinant cytochrome c from the Thermus thermophilus cy tochrome c552 gene may be generally useful for expression of alien cyto chrome c genes in E. coli. Expand