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Comparative Study
. 1987 Sep 15;246(3):787-9.
doi: 10.1042/bj2460787.

Haem disorder in two myoglobins: comparison of reorientation rate

A Bellelli  1 , R Foon, F Ascoli, M Brunori
Affiliations
Comparative Study

Haem disorder in two myoglobins: comparison of reorientation rate

A Bellelli et al. Biochem J. .

Abstract

The globins from sperm whale and from Aplysia limacina myoglobins were reconstituted by addition of stoichiometric ferric protohaem and the Soret c.d. was followed as a function of time. For both reconstituted proteins, the Soret c.d. changes with time, reflecting haem reorientation inside its pocket, as previously described [Aojula, Wilson & Drake (1986) Biochem. J. 237, 613-616] for sperm whale myoglobin. The time course of the c.d. transition is found to be approx. 10 times faster in Aplysia than in sperm whale myoglobin, a result which is in agreement with the known structural and physicochemical properties of the two myoglobins; furthermore, these results confirm that c.d. and n.m.r. data on haem orientation in haemoproteins reflect the same molecular phenomenon.

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