Human hemoglobin has been shown to contain a high- as well as a low-affinity binding site for cupric ion on each of its constitutent β chains. The copper that is bound to the low-affinity site has been implicated in the selective oxidation of the β hemes. In the present work a low-affinity binding site for cupric ion has been located within 10 Å of the heme iron in human hemoglobin. It is suggested that the proximal histidine is involved in the binding of copper at this site and that it participates in the oxidation of heme iron and reduction of cupric ion.

ANTHOLINE W., E., Basosi, R., HYDE J., S., & Taketa, F. (1984). Interaction Between Low-Affinity Cupric Ion and Human Methemoglobin. JOURNAL OF INORGANIC BIOCHEMISTRY, 21(2), 125-136 [10.1016/0162-0134(84)85045-X].

Interaction Between Low-Affinity Cupric Ion and Human Methemoglobin

BASOSI, RICCARDO;
1984

Abstract

Human hemoglobin has been shown to contain a high- as well as a low-affinity binding site for cupric ion on each of its constitutent β chains. The copper that is bound to the low-affinity site has been implicated in the selective oxidation of the β hemes. In the present work a low-affinity binding site for cupric ion has been located within 10 Å of the heme iron in human hemoglobin. It is suggested that the proximal histidine is involved in the binding of copper at this site and that it participates in the oxidation of heme iron and reduction of cupric ion.
ANTHOLINE W., E., Basosi, R., HYDE J., S., & Taketa, F. (1984). Interaction Between Low-Affinity Cupric Ion and Human Methemoglobin. JOURNAL OF INORGANIC BIOCHEMISTRY, 21(2), 125-136 [10.1016/0162-0134(84)85045-X].
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/31795
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