Hemoglobin from a deep-sea hydrothermal-vent copepod.

Deep-sea hydrothermal-vent fauna live in a highly variable environment where oxygen levels can be very low, and carbon dioxide and sulfide can reach high concentrations (1). These conditions are harsh for most aerobic metazoans, yet copepods can be abundant at hydrothermal vents. Here we report the structure and functional properties of hemoglobin extracted from the copepod Benthoxynus spiculifer, which was found in large numbers in a paralvinellid/gastropod community collection made during a cruise to the Juan de Fuca Ridge in 1998. Although hemoglobin has been reported in some littoral copepods (2), this is the first study of the structure and functional properties of copepod hemoglobin. Hemoglobin represents about 60% of the total soluble proteins extracted from B. spiculifer, and although it imparts a red color to the copepod, it does not provide a significant storage pool of oxygen. It is a 208-kDa protein, composed of 14 globin chains--7 of 14.3 kDa and 7 of 15.2 kDa. The hemoglobin has a very high and temperature-sensitive oxygen affinity, with no cooperativity or Bohr effect. These properties are adaptive for an animal living in a low-oxygen environment in which the primary function of the hemoglobin is most likely oxygen acquisition to support aerobic respiration.