Rimicaris exoculata is a caridean shrimp from the family Alvinocarididae which forms the dominant species around deep‐sea hydrothermal vents from the Mid‐Atlantic Ridge (MAR). Seeking respiratory adaptations to the hydrothermal environment, we have analysed the oxygen‐binding properties of Rimicaris hemocyanin (Hc) in relation with temperature, pH, and lactate variations. Rimicaris native Hc is mostly composed of hexamers. It showed a high oxygen affinity (P50 approximately 3 Torr at pH 7.5, 15°C), a large Bohr effect (ΔlogP50/ΔpH = −1.87 ± 0.25, n = 6), a moderate lactate effect (ΔP50/Δlog[lac] = −0.12) and almost no temperature effect (ΔH = −1.23 kJ.mol−1 15–35°C). Most surprisingly, dialysis of native hemolymph elicited a large increase of HC‐O2 affinity, an effect opposite to the usual trend observed for crustacean Hcs. Moreover, this increase in affinity could be reversed by adding an ultrafiltrate of native hemolymph to a dialysed sample, thus unveiling the existence of a dialysable yet unknown cofactor which decreases Hc‐oxygen affinity. J. Exp. Zool. 277:357–364, 1997. © 1997 Wiley‐Liss, Inc.