Energetics of heme binding to native and denatured states of cytochrome b562.

@article{Robinson1997EnergeticsOH,
  title={Energetics of heme binding to native and denatured states of cytochrome b562.},
  author={Clifford Ralph Robinson and Yuliang Liu and James A. Thomson and Julian Munson Sturtevant and Stephen G Sligar},
  journal={Biochemistry},
  year={1997},
  volume={36 51},
  pages={
          16141-6
        }
}
Cytochrome b562 is a four-helix bundle protein containing a noncovalently bound b-type heme prosthetic group. For the first time, energetics of heme binding to an apocytochrome were measured by isothermal titration calorimetry. The heme is tightly bound to native apocytochrome b562, with a dissociation constant (Kd) of approximately 9 nM (DeltaG degrees = 11 kcal mol-1) at 25 degrees C. Unexpectedly, the thermally denatured apoprotein is also capable of specifically binding heme with modest… CONTINUE READING
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