The hemichromogen form of the isolated subunits of hemoglobin

Enrico Bucci; Clara Fronticelli

doi:10.1016/0005-2795(71)90073-0

The hemichromogen form of the isolated subunits of hemoglobin

Enrico Bucci, Clara Fronticelli

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	170-177
Number of pages	8
Journal	BBA - Protein Structure
Volume	243
Issue number	2
DOIs	https://doi.org/10.1016/0005-2795(71)90073-0
State	Published - Aug 27 1971
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

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10.1016/0005-2795(71)90073-0

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abstract = "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.",

author = "Enrico Bucci and Clara Fronticelli",

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AU - Bucci, Enrico

AU - Fronticelli, Clara

N1 - Funding Information: The authorsa rei ndebtedto Dr. Morris Reichlinf or his assistancien performing and interpretinsgo meo f the immunologiceaxl perimentas,ls od onei n his laboratory. This work was supporteidn part by U.S. Public HealthS erviceg rantsH E 13178 and HE 13164f romthe NationalI nstituteo f Health,U .S. Public Health Service.

PY - 1971/8/27

Y1 - 1971/8/27

N2 - 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.

AB - 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.

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The hemichromogen form of the isolated subunits of hemoglobin

Abstract

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