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Moessbauer spectroscopic studies of hemerythrin from Phascolosoma lurco (syn. Phascolosoma Arcuatum)
Journal article   Peer reviewed

Moessbauer spectroscopic studies of hemerythrin from Phascolosoma lurco (syn. Phascolosoma Arcuatum)

P.E. Clark and J. Webb
Biochemistry, Vol.20(16), pp.4628-4632
1981
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Abstract

Hemerythrin from coelomic cells of Phascolosoma lurco (syn. P. arcuatum) was isolated by gel filtration as two components, hemerythrin-I (25%) and hemerythrin-I1 (75%). The Mossbauer spectrum of oxyhemerythrin-I1 consisted of two pairs of lines of the same isomer shift (0.5 mm s-I) corresponding to Fe(II1) but different quadrupole splitting (1 -01 and 2.02 mm s-I). Application of a 2.5-T magnetic field at 4.2K caused no significant spectral broadening. The 2Fe.02 binding site thus contains two nonequivalent high-spin Fe(II1) ions that are antiferromagnetically coupled. The Mossbauer spectra of the minor component, hemerythrin-I, indicated an identical binding site. On deoxygenation, the spectrum was dominated by a simple quadrupole split doublet corresponding to Fe(II), indicating that the binding site in this derivative contains two identical Fe(I1) ions that interact only weakly, if at all. The Mossbauer spectra of azidohemerythrin-I1 indicated that this derivative also contains a pair of antiferro- magnetically coupled Fe(II1) ions with the same isomer shift (0.5 mm s-') but quadrupole splittings (1.40 and 1.96 mm s-') that are not identical with those in oxyhemerythrin.

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Citation topics
2 Chemistry
2.22 Inorganic & Nuclear Chemistry
2.22.1421 Metal Complex Reactivity
Web Of Science research areas
Biochemistry & Molecular Biology
ESI research areas
Biology & Biochemistry
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