Determining Rieske cluster reduction potentials

@article{Brown2008DeterminingRC,
  title={Determining Rieske cluster reduction potentials},
  author={Eric Brown and Rosmarie Friemann and Andreas Karlsson and Juanito V. Parales and Manon Couture and Lindsay D. Eltis and S Ramaswamy},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2008},
  volume={13},
  pages={1301-1313}
}
The Rieske iron–sulfur proteins have reduction potentials ranging from −150 to +400 mV. This enormous range of potentials was first proposed to be due to differing solvent exposure or even protein structure. However, the increasing number of available crystal structures for Rieske iron–sulfur proteins has shown this not to be the case. Colbert and colleagues proposed in 2000 that differences in the electrostatic environment, and not structural differences, of a Rieske proteins are responsible… Expand
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References

SHOWING 1-10 OF 69 REFERENCES
Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state.
TLDR
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
Protein control of iron-sulfur cluster redox potentials.
TLDR
These calculations provide the first successful quantitative modeling of the protein control of iron-sulfur cluster redox potentials and show that the potentials in these proteins are tuned in part by varying the access of solvent water to the neighborhood of the cluster. Expand
A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins.
TLDR
The crystal structure of BphF, the Rieske-type ferredoxin associated with biphenyl dioxygenase, has structural features consistent with a minimal and perhaps archetypical Rieskes protein. Expand
Density functional calculation of pKa values and redox potentials in the bovine Rieske iron-sulfur protein
TLDR
A density functional/continuum electrostatics calculation of the pKa values of the histidines in the Rieske iron-sulfur center provides a complete picture of the coupling of proton and electron binding, showing strongly cooperative binding of protons at electrode potentials near the redox midpoint potential of the cluster. Expand
Roles of the disulfide bond and adjacent residues in determining the reduction potentials and stabilities of respiratory-type Rieske clusters.
TLDR
The effects of similar mutations on cluster potential, pK values, and stability are characterized comprehensively in the isolated Rieske domain of the bovine protein. Expand
Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential.
TLDR
The results indicate that the 450 mV spread in reduction potential of Rieske clusters of dioxygenase-associated ferredoxins and mitochondrial bc(1) complexes is not due to significant differences in their solvent exposure. Expand
Expression of the Solfolobus acidocaldarius Rieske iron sulfur protein II (SOXF) with the correctly inserted [2FE-2S] cluster in Escherichia coli.
TLDR
The presented data demonstrate that the structure of the recombinant protein is very similar or identical to the authentic protein making this a powerful model system for the studies of Rieske proteins by site directed mutagenesis. Expand
The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 A resolution.
TLDR
The main domain of soxF and part of the cluster-binding domain, though structurally related, show a significantly divergent structure with respect to topology, non-covalent interactions and surface charges, reflecting a different topology of the soxM complex compared to eucaryal bc complexes. Expand
Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters.
TLDR
These studies provide a detailed structure-function dissection of the role of hydrogen bonds in tuning the redox potentials of [2Fe-2S] clusters and provide a molecular framework for understanding the role hydrogen bonds to the cluster play in tuning thermodynamic properties, and hence the rate of this bioenergetic reaction. Expand
Characterization and Crystallization of the Lumen Side Domain of the Chloroplast Rieske Iron-Sulfur Protein*
A soluble, 139-residue COOH-terminal polypeptide fragment of the Rieske iron-sulfur protein of the cytochrome b6f complex from spinach chloroplasts was obtained by limited proteolysis of the complexExpand
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