ABSTRACT
Pioneering work on metalloenzymes and proteins, stretching back to before 1900, was naturally concentrated on the readily available and conspicuously colored hemoproteins, such as hemoglobin, myoglobin, peroxidase, and catalase. The study of a wider range of metalloproteins and enzymes began to merge under the banner of bioinor ganic chemistry (or inorganic biochemistry) from the 1950s, in parallel with the development of many of our current ideas of coordination chemistry. The new subject enjoyed a golden period of intellectual excitement in the 1960s. Structure determina tions were reported for myoglobin (as the very first protein) in 1960, the protein-free coenzyme form of Bi2 (with its unexpected and relatively stable Co-C bond) in 1961, several forms of hemoglobin (revealing the subtle conformation changes underlying the cooperative interaction between the four Fe atoms) over the period 1964-1968, and lysozyme (as the first true but nonmetallic enzyme) in 1965. Cell-free fixation of nitrogen was achieved in 1960, methods for isolating and purifying cytochrome oxi dase developed during 1958-1961, and the membrane-bound knobs of the mitochon dria (see Sec. 2 ) shown to have ATPase activity in 1960, followed by development of the chemiosmotic theory for using the proton gradient to drive ATP synthesis in 1961-1962. For introductory references, see the relevant chapters.
