Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.

@article{Baker1997CytochromeCS,
  title={Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.},
  author={Simon C Baker and N F Saunders and Anthony C. Willis and Stuart Ferguson and J{\'a}nos Hajdu and Vilmos F{\"u}l{\"o}p},
  journal={Journal of molecular biology},
  year={1997},
  volume={269 3},
  pages={440-55}
}
The central tunnel of the eight-bladed beta-propeller domain of cytochrome cd1 (nitrite reductase) is seen, from a 1.28 A resolution structure, to contain hydrogen donors and acceptors that are satisfied by interaction either with water or the d1 haem. The d1 haem, although bound by an extensive network of hydrogen bonds, is not distorted in its binding pocket and is confirmed to have exactly the dioxoisobacteriochlorin structure proposed from chemical studies. A biological rationale is… CONTINUE READING
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