Journal article
Ligand-dependent redox chemistry of Glycera dibranchiata hemoglobin
Biochimica et biophysica acta, Protein structure and molecular enzymology, v 828(3), pp 362-368
1985
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The
trans-1,2-diaminocyclohexane-
N,
N,
N′,
N′-tetraacetatoferrate(III)/(II) couple was used as a redox buffer-mediator to determine that the redox potential of the monomeric hemoglobin of
Glycera dibranchiata is +0.153 ± 0.008 V at 27°C in 0.1 M (pH 7.8) phosphate. The value is similar to that for
Aplysia myoglobin, which also lacks distal histidine. Correlation of
E
0′ with log
p
1
2
(
O
2
)
is discussed. Hexacyanoferrate(II) binds to the protein, resulting in an unusual enhancement of oxygen affinity. The binding of azide anion to the aquomet-protein has been studied by a spectropotentiostatic method and by the conventional spectrophotometric technique, and the results are interpreted in terms of an ionic dependence.
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Details
- Title
- Ligand-dependent redox chemistry of Glycera dibranchiata hemoglobin
- Creators
- A.W. Addison - Drexel UniversityS. Burman - Drexel University
- Publication Details
- Biochimica et biophysica acta, Protein structure and molecular enzymology, v 828(3), pp 362-368
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:A1985AHM2300020
- Scopus ID
- 2-s2.0-0010290469
- Other Identifier
- 991019173625404721
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InCites Highlights
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- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics