Abstract
The respiratory enzyme of Warburg and Keilin1,2 has remained an enigma since its discovery by these two pioneers in the field of cell respiration. Warburg identified the heme nature of the enzyme while Keilin perceived the chain of electron transfer components as an integral factor in cell respiration. Aside from certain further elaborations of the function of cytochromes in energy coupling and in respiratory control, the molecular mechanisms for oxygen reduction and energy conservation have remained largely in “the black box” status,3 where a number of structural and functional properties were ascribed to the system in order to be consistent with the ingenious hypothesis of transmembrane charge transfer according to Lundegårdh and Mitchell.3 There was one good reason for the popularity of “the black box” approach—the lack of protein crystals and appropriate derivatives for high resolution X-ray crystallography of electron transfer components. Thus, the dearth of knowledge on the nature of the iron and copper atoms, their ligands, and interatomic distances has rendered incomplete, detailed explanations of electron transfer mechanisms and energy conservation.
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Chance, B., Powers, L., Ching, Y. (1982). Structure and Function of the Redox Site of Cytochrome Oxidase. In: Bossa, F., Chiancone, E., Finazzi-Agrò, A., Strom, R. (eds) Structure and Function Relationships in Biochemical Systems. Advances in Experimental Medicine and Bioligy, vol 148. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9281-5_9
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