Helix switching of a key active-site residue in the cytochrome cbb3 oxidases.

@article{Hemp2005HelixSO,
  title={Helix switching of a key active-site residue in the cytochrome cbb3 oxidases.},
  author={James Hemp and Caroline E. Christian and Blanca Barquera and Robert B Gennis and Todd J. Mart{\'i}nez},
  journal={Biochemistry},
  year={2005},
  volume={44 32},
  pages={
          10766-75
        }
}
In the respiratory chains of mitochondria and many aerobic prokaryotes, heme-copper oxidases are the terminal enzymes that couple the reduction of molecular oxygen to proton pumping, contributing to the protonmotive force. The cbb(3) oxidases belong to the superfamily of enzymes that includes all of the heme-copper oxidases. Sequence analysis indicates that the cbb(3) oxidases are missing an active-site tyrosine residue that is absolutely conserved in all other known heme-copper oxidases. In… CONTINUE READING
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