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Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins
Journal article   Open access   Peer reviewed

Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins

T J DiFeo and A W Addison
Biochemical journal, v 260(3), pp 863-871
15 Jun 1989
PMID: 2764907
url
https://doi.org/10.1042/bj2600863View
Published, Version of Record (VoR)Open Access (License Unspecified) Open

Abstract

Animals Circular Dichroism Heme - metabolism Hemoglobins - metabolism Isoelectric Focusing Polychaeta - metabolism
The five major components of the monomeric haemoglobin from Glycera dibranchiata were separated and characterized by absorption spectroscopy, isoelectric focusing, azide-binding affinities and nitrosyl autoreduction kinetics. The differences found among the components are discussed in terms of haem-pocket variations. In addition, the Fourier-transform i.r. spectra of pooled monomeric haemoglobin carbonyl (HbmCO) and the major component carbonyl are reported. The c.d. spectra of the carbonyl and azide derivatives of the five components are compared and found to be similar. The c.d. spectra of myoglobin(II) carbonyl [Mb(II)CO] and of apomyoglobin (apoMb) reconstituted with a symmetric synthetic iron porphyrin carbonyl, meso-tetra-(p-carboxyphenyl)porphinatoiron(II) carbonyl [TCPPFe(II)CO], are compared with the c.d. spectra of pooled HbmCO and its TCPPFe(II)CO analogue. HbmTCPPFe(II)CO shows a negative Soret c.d. band whereas MbTCPPFe(II)CO produces both a negative and a positive Soret c.d. band. Displacement of the symmetric porphyrin by 8-anilinonaphthalene-1-sulphonate and the resulting fluorescence emission are reported.

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Biochemistry & Molecular Biology
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