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- W1983201430 abstract "Absorption spectra of ferrous and ferric haem a and haem a compounds with nitrogenous ligands (pyridine, 4-methylimidazole, cyanide, human and bovine serum albumins, human apohaemoglobin, horse apomyoglobin and horse-radish apoperoxidase) as well as their carbon monoxide compounds are described. The absorption spectra of the haemoproteins provide a good model for bacterial cytochrome a 1 , but not for cytochrome a and especially not for cytochrome a 3 . Both cytochromes a and a 3 differ from the model haemoproteins in the position of the α -band of the ferrous compound. Cytochrome a 3 differs from them, moreover, in that carbon monoxide shifts its α -band towards the blue, not towards the red, and in its much higher ratio of extinction of the Soret band to that of the α -band. The type of linkage of a protein to haematin a appeared to differ in several instances from the type of linkage of the same protein to protohaematin. The characteristic spectroscopic differences between haemoglobin, haemalbumin and haemochromes, or between human and bovine haemalbumin, found in the protohaem series, are absent in the haem a series. We have found no evidence for a reversible combination of haem a -globin with molecular oxygen; nor had the compound of haem a with the apoenzyme of horse-radish peroxidase strong peroxidative activity." @default.
- W1983201430 created "2016-06-24" @default.
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- W1983201430 date "1962-01-09" @default.
- W1983201430 modified "2023-10-06" @default.
- W1983201430 title "Haem a compounds as models for cytochromes of group a - I. Absorption spectra of haem a compounds with proteins and other nitrogenous ligands" @default.
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- W1983201430 doi "https://doi.org/10.1098/rspb.1962.0003" @default.
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