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- W2037943430 abstract "Several pH-dependent low-spin ferric haem forms are identified in a frozen solution of the ferric 121Cys→Ser mutant of Drosophila melanogaster haemoglobin (DmHb1*) using electron paramagnetic resonance (EPR) techniques. Different forms with EPR parameters typical of bis-histidine coordinated haem iron centers were observed. Strong pH-dependent changes in the EPR signatures were observed related to changes in the haem pocket. The pulsed EPR data indicate that both the distal and proximal histidine exhibit a large libration around the Fe–NHis axis. The resonance Raman spectra of the CO-ligated ferrous form of Drosophila melanogaster haemoglobin are typical of an open conformation, with little stabilization of the CO ligand by the surrounding amino-acid residues. The EPR data of the cyanide-ligated ferric DmHb1* indicates a close similarity with cyanide-ligated ferric myoglobin. The structural characteristics of DmHb1* are found to clearly differ from those of other bis-histidine-coordinated globins. A combined resonance Raman, continuous-wave and pulsed electron paramagnetic resonance study reveals a significant flexibility of the proximal and distal histidine ligands of the haem iron in Drosophila melanogaster haemoglobin." @default.
- W2037943430 created "2016-06-24" @default.
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- W2037943430 date "2009-01-01" @default.
- W2037943430 modified "2023-09-25" @default.
- W2037943430 title "Unusual flexibility of distal and proximal histidine residues in the haem pocket of Drosophila melanogaster haemoglobin" @default.
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- W2037943430 doi "https://doi.org/10.1039/b902059b" @default.
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