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Journal article
Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins
Biochemical journal, v 260(3), pp 863-871
15 Jun 1989
PMCID: PMC1138756
PMID: 2764907
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Abstract
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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Details
- Title
- Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins
- Creators
- T J DiFeo - Drexel UniversityA W Addison - Drexel University
- Publication Details
- Biochemical journal, v 260(3), pp 863-871
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:A1989AB92400033
- Scopus ID
- 2-s2.0-0024970661
- Other Identifier
- 991019173795004721
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- Web of Science research areas
- Biochemistry & Molecular Biology