Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.
- M. Lah, M. M. Dixon, K. Pattridge, W. Stallings, J. Fee, M. Ludwig
- ChemistryBiochemistry
- 7 February 1995
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.
Kinetic studies of superoxide dismutases: properties of the manganese-containing protein from Thermus thermophilus
- C. Bull, E. Niederhoffer, Tatsuro Yoshida, J. Fee
- Chemistry
- 1 May 1991
The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
- Hsin-Yang Chang, J. Hemp, Ying Chen, J. Fee, R. Gennis
- BiologyProceedings of the National Academy of Sciences
- 22 September 2009
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.
Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function
- J. Fee
- BiologyMolecular 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.
Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus
- E. Niederhoffer, C. Naranjo, K. Bradley, J. Fee
- BiologyJournal of Bacteriology
- 1 April 1990
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.
High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment
- T. Tiefenbrunn, Wei Liu, V. Cherezov
- ChemistryPLoS ONE
- 21 July 2011
The structure of ba3-oxidase reveals new information about the positioning of the enzyme within the membrane and the nature of its interactions with lipid molecules, and provides insight into the mechanisms of electron transfer, oxygen diffusion into the active site, reduction of oxygen to water, and pumping of protons across the membrane.
High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison.
- L. Hunsicker-Wang, A. Heine, J. Fee
- ChemistryBiochemistry
- 24 May 2003
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.
Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state.
- Y. Zu, M. Couture, J. Hirst
- ChemistryBiochemistry
- 7 October 2003
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.
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