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Functional SAXS study reveals differences in dioxygen binding among molluscan haemocyanins, suggesting structural variation.
The effects of conformational rearrangements on dioxygen binding to molluscan haemocyanins have been investigateted by small-angle X-ray scattering (SAXS). The SAXS patterns of the oxygenated and deoxygenated two forms of Octopus vulgaris haemocyanin are significantly different; whereas the patterns of the two forms of Rapana thomasiana haemocyanin are almost superimposable. A program has been developed, based on the differences in molecular dimensions, in order to simulate the effects observed in the investigaion.
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M. et al. (1997) studied this question.
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