Effects of pH on the Rieske protein from Thermus thermophilus: a spectroscopic and structural analysis.

@article{Konkle2009EffectsOP,
  title={Effects of pH on the Rieske protein from Thermus thermophilus: a spectroscopic and structural analysis.},
  author={Mary E. Konkle and Sarah K Muellner and Anika L Schwander and Michelle M Dicus and Ravi Pokhrel and R David Britt and Alexander Bryan Taylor and Laura M. Hunsicker-Wang},
  journal={Biochemistry},
  year={2009},
  volume={48 41},
  pages={9848-57}
}
The Rieske protein from Thermus thermophilus (TtRp) and a truncated version of the protein (truncTtRp), produced to achieve a low-pH crystallization condition, have been characterized using UV-visible and circular dichroism spectroscopies. TtRp and truncTtRp undergo a change in the UV-visible spectra with increasing pH. The LMCT band at 458 nm shifts to 436 nm and increases in intensity. The increase at 436 nm versus pH can be fit using the sum of two Henderson-Hasselbalch equations, yielding… CONTINUE READING
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