Intensive studies of iron‐sulfur proteins were begun only a decade or so ago but many biological and physicochemical data have since been accumulated and summarized1–5. As a result of the very recent X‐ray analyses of the structures of rubredoxin6, ferredoxin (Peptococcus aerogenes)7 and the Chromatium vinosum high potential iron protein (Hipip)8, it has become possible to review our understanding of the nature and function of the inorganic chromophores in these proteins; to relate these findings to ‘model’ systems of varying relevance; but of more general interest, to comment on redox processes in biological systems particularly with respect to what might be termed electron transfer—allosteric effects in metalloenzymes.
|Original language||English (US)|
|Number of pages||10|
|Journal||Angewandte Chemie International Edition in English|
|State||Published - May 1973|
- Bioinorganic chemistry
- Iron–sulfur proteins
ASJC Scopus subject areas