Specific effects of thiosulphate and L-lactate on hemocyanin-O2 affinity in a brachyuran hydrothermal vent crab

The hydrothermal vent crab Bythograea thermydron Williams (Brachyura: Bythograeidae) is exposed to high environmental concentrations of hydrogen sulphide. Hydrogen sulphide has previously been shown to be oxidized to a non-toxic form, thiosulphate (S₂O₃^2-), that accumulates in the hemolymph (to concentrations>1 mmoll^-1). Hemocyanin-oxygen (Hc-O₂) affinity was determined in dialysed, fresh or frozen hemolymph samples from B. thermydron. Although freezing is known to alter the affinity or cooperativity of some decapod crustacean hemocyanins, neither Hc-O₂ affinity nor cooperativity was significantly altered in B. thermydron hemolymph samples that had been frozen, consistent with previous findings. Oxygen affinity of B. thermydron hemocyanin was significantly increased by the presence of L-lactate. Likewise, Hc-O₂ affinity was significantly increased by the presence of 1.5 mmol S₂O₃^2- I^-1. The magnitude of this effect was the same as for similar concentrations of L-lactate. This specific effect of S₂O₃^2- does not appear to be a general property of crustacean hemocyanins, as there was no significant effect of S₂O₃^2- on Hc-O₂ affinity or cooperativity in dialysed hemolymph samples from the brachyuran crabs Cancer anthonyi Rathbun and C. antennarius Stimpson, or the thalassinid ghost shrimp Callianassa californiensis Dana. In the context of high environmental sulphide concentrations coupled with low P_O2, and the subsequent accumulation of S₂O₃^2- in crab hemolymph, the increase in Hc-O₂ affinity due to thiosulphate appears to be an adaptive response in B. thermydron.