The hemichromogen form of the isolated subunits of hemoglobin

Enrico Bucci, Clara Fronticelli

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


When the iron atom of the isolated α chains of human hemoglobin is oxidized a conformational change occurs which is produced by the binding to the ferric heme of a second nitrogen base present in the globin. The conformational change is irreversible and immunological tests reveal that the interaction of the ferric α chains with ferrous β chains is impaired. The physicochemical characteristics of this compound and the comparison of its absorption spectrum in the visible and Soret region with that of ferric hemoglobin in the presence of imidazole suggest that in the ferric α chains the "distal" histidine might be the nitrogen base which binds to the heme.

Original languageEnglish (US)
Pages (from-to)170-177
Number of pages8
JournalBBA - Protein Structure
Issue number2
StatePublished - Aug 27 1971
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)


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