1. S. De Vries, S. P. J. Albracht, and F. J. Leeuwerik, The multiplicity and stoichiometry of the prosthetic groups in QH2: cytochrome c oxidoreductase as studied by EPR, Biochim. Biophys. Acta 546: 316 (1979).
2. H. G. Heidrich, S. P. J. Albracht and D. Bäckström, Two iron-sulfur centers in mitochondrial membranes from beef heart as prepared by free-flow electrophoresis, FEBS Letters 95: 314 (1978).
3. J. S. Rieske, R. E. Hansen, and W. S. Zaugg, Studies on the electron transfer system. LVII. Properties of a new oxidation-reduction component of the respiratory chain as studied by electron paramagnetic resonance spectroscopy, J. Biol. Chem. 239: 3017 (1964).
4. F. J. Ruzicka and H. Beinert, The soluble “high potential” type iron-sulfur protein from mitochondria is aconitase, J. Biol. Chem. 253: 2514 (1978).
5. T. A. Kent, J. L. Dreyer, M. H. Emptage, I. Moura, J. J. G. Moura, B. H. Huynh, A. V. Xavier, J. LeGall, H. Beinert, W. H. Orme-Johnson, and E. Münck, Evidence for novel three iron center in two ferredoxins, aconitase and glutamate synthase, in: “Interaction between iron and protein in oxygen and electron transport,” C. Ho, ed., Pergamon Press, London (1981).