Oxygen Binding to a Model for the Active Site in Cobalt-Substituted Hemoglobin

Frank S. Molinaro, James A. Ibers, Robert G. Little

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Cobalt(II) porphyrin complexes, which are models for the active site in cobalt-substituted hemoglobin, CoHb, have been synthesized and characterized by NMR and visible spectroscopy. The model compounds are based on the tetratolylporphyrin ring system and have covalently attached chains which terminate in a pyridyl ring. The cobalt(II) complexes of these “looping-over porphyrins” react reversibly with dioxygen at low temperatures. The oxygen affinities of these compounds have been measured and the results compared with those obtained with other porphyrins and the protein. Our results indicate that there is negligible enhancement of the oxygen affinity of a cobalt(II) porphyrin when an axial base is covalently attached.

Original languageEnglish (US)
Pages (from-to)5628-5632
Number of pages5
JournalJournal of the American Chemical Society
Volume99
Issue number17
DOIs
StatePublished - Jan 1 1977

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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