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Our results indicate that both SdhB-R205 and SdhB-K230 play important roles in fine tuning the reduction potential of both the [3Fe 4S] cluster and the heme.
For tuning the reduction efficiency flow rates up to 200 μl/min were applied.
Understanding the origin of this variance and the structural features involved in tuning the reduction potential are of great importance.
Mutational analyses have been extensively used to reveal features that are important in tuning the reduction potential.
Computational studies showed that the cluster distortions caused by the protein environment play a prominent role in tuning the reduction potential of the center.
B3LYP density functional methods have been used in combination with broken symmetry to analyze factors that are important in tuning the reduction potential of Rieske proteins.
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The substituents employed generally are (i) electron-withdrawing to tune the reduction potential to the desirable range (near +0.3 V vs NHE), and/or (ii) lipophilic to target the interior of lipid bilayer membranes and/or the blood brain barrier.
The substituents employed generally are (i) electron-withdrawing to tune the reduction potential to the desirable range (near +0.3V vs NHE), and/or (ii) lipophilic to target the interior of lipid bilayer membranes and/or the blood-brain barrier.
This effect is important in fine-tuning the reduction potential of proteins with two clusters.
Several factors have been reported to be important in fine-tuning the reduction potentials of ferredoxins.
Several studies have shown the importance of the protein environment in fine-tuning the reduction potentials of metal centers.
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