Faculty Collaboration Database

Interaction between low-affinity cupric ion and human methemoglobin. J Inorg Biochem 1984 Jun;21(2):125-36

Date

06/01/1984

Pubmed ID

6330294

DOI

10.1016/0162-0134(84)85045-x

Scopus ID

2-s2.0-0021162268 (requires institutional sign-in at Scopus site)   9 Citations

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 beta chains. The copper that is bound to the low-affinity site has been implicated in the selective oxidation of the beta hemes. In the present work a low-affinity binding site for cupric ion has been located within 10 A 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.

Author List

Antholine WE, Basosi R, Hyde JS, Taketa F

MESH terms used to index this publication - Major topics in bold

Animals
Binding Sites
Cations, Divalent
Cats
Copper
Electron Spin Resonance Spectroscopy
Heme
Humans
Kinetics
Methemoglobin
Protein Binding