Iron‐Sulfur Proteins: Structural Chemistry of Their Chromophores and Related Systems

Ronald Mason, J. A. Zubieta

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)390-399
Number of pages10
JournalAngewandte Chemie International Edition in English
Volume12
Issue number5
DOIs
StatePublished - May 1973
Externally publishedYes

Keywords

  • Bioinorganic chemistry
  • Chromophores
  • Iron–sulfur proteins
  • Proteins

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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