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- W2023389467 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 E0′ with log p12(O2) 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." @default.
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- W2023389467 title "Ligand-dependent redox chemistry of Glycera dibranchiata hemoglobin" @default.
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