High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.

@article{Bonagura2003HighresolutionCS,
  title={High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.},
  author={Christopher A. Bonagura and Banerjee Bhaskar and Hideaki Shimizu and Huiying Li and Munirathinam Sundaramoorthy and Duncan E. McRee and David B. Goodin and Thomas L Poulos},
  journal={Biochemistry},
  year={2003},
  volume={42 19},
  pages={5600-8}
}
Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis absorption and electron paramagnetic resonance spectroscopies before and after data collection to… CONTINUE READING
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