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Abstract

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.

Keywords

Iron Atom Haem Iron Haem Protein Porphyrin Ring Pyrrole Nitrogen 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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