PMID: 205264Mar 28, 1978

Oxygenation and EPR spectral properties of Aplysia myoglobins containing cobaltous porphyrins

Biochimica Et Biophysica Acta
M Ikeda-SaitoT Yonetani

Abstract

Cobalt myoglobins (Aplysia) have been reconstituted from apo-myoglobin (Aplysia) and proto-, meso-, and deutero-cobalt porphyrins. Each of them showed the 30--60 times lower oxygen affinity than those of the corresponding cobalt myoglobins (Sperm whale). Kinetic investigation of their oxygenation by the temperature-junp relaxation technique showed that the low oxygen affinity of cobalt myoglobin (Aplysia) is due to a large dissociation rate constant. the electron paramagnetic resonance (EPR) spectrum of oxy cobalt myoglobin (Aplysia) is affected by the replacement of H2O with D2O, suggesting a possible interaction between the bound oxygen and the neighboring hydrogen atom. A low temperature photodissociation study showed that the product of photolysis of oxy cobalt myoglobin (Aplysia) gives an EPR spectrum different from that of the deoxy-cobalt myoglobin (Aplysia) and from that of the photolysed form of oxy-cobalt myogloin (Sperm whale). These observations suggest that in oxy-cobalt myoglobin (Aplysia) the bound oxygen might interact with amino acid adjacent to it, but the interaction is weaker than that in oxy cobalt myoglobin (Sperm whale).

References

Oct 1, 1970·Proceedings of the National Academy of Sciences of the United States of America·B M Hoffman, D H Petering
Jul 21, 1999·Proceedings of the National Academy of Sciences of the United States of America·D BonnetS R Riddell
Feb 1, 2007·Disease Markers·Amit KumarKalpana Luthra

Citations

Feb 25, 2010·Acta Crystallographica. Section D, Biological Crystallography·Takao KuwadaFumio Shishikura
May 7, 2013·Biochimica Et Biophysica Acta·T Yonetani, Kenji Kanaori

Related Concepts

Metazoa
Aplysia
Carbon Monoxide
Cobalt
Electron Spin Resonance Spectroscopy
Myoglobin
Dioxygen
Porphyrins
Plasma Protein Binding Capacity
Right Whale, North Atlantic

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