Hemoglobin Kinetics of the Galápagos Rift Vent Tube Worm Riftia pachyptila Jones (Pogonophora; Vestimentifera)

Kinetics of the reactions of Riftia pachyptila hemoglobin with oxygen were followed spectrophotometrically by stopped-flow and laser flash photolysis techniques. The rate of oxygen dissociation increases eightfold over the range of 5 degrees to 20 degrees C (k = 2.2 sec(-1)at 10 degrees C). Oxygen recombination after flash photolysis was biphasic. The rates of both slow and fast phases of the reaction were independent of temperature from 0 degrees to 20 degrees C(k'fast = 7 x 10(6); k'slow = 1 x 16(6) liter mole (-1) sec(-1)). As the oxygen affinity is relatively temperature independent, analysis in terms of the two-state model of cooperativity requires that the conformational equilibrium constant L decrease by about 50-fold between 3 degrees and 15 degrees C.