Haem proteins are widely distributed in cellular systems, catalysing a variety of reactions, primarily oxidation-reduction processes essential for respiration and production of metabolic energy. A variety of haem proteins with widely different biological reactivities and specificities are known (see reference 87). However, three-dimensional structures have been determined by diffraction methods only for myoglobins10–13,88, haemoglobins of both mammalian and lower-order species14–18,89, calf-liver calf-liver cytochrome b521,90, and oxidised horse heart19 and reduced bonito-tuna20 cytochrome c. Structural investigations have been initiated on yeast cytochrome c peroxidase23,24. Also, a variety of difference Fourier studies have been carried out on sperm-whale myoglobin66,70,91–3 and haemoglobins94–7.


Iron Atom Haem Iron Haem Protein Porphyrin Ring Pyrrole Nitrogen 
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Copyright information

© Palgrave Macmillan, a division of Macmillan Publishers Limited 1975

Authors and Affiliations

  • C. A. Mcauliffe
    • 1
  1. 1.Institute of Science and TechnologyUniversity of ManchesterUK

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