The clam Solemya reidi, which survives in sulfide-rich sediments, houses intracellular sulfide-oxidizing bacteria as symbionts in its gills. The gill bacteriocytes also contain a high concentration of cytoplasmic hemoglobin. Although the in situ hemoglobin optical spectrum was not altered in the presence of hydrogen sulfide, hemoglobin deoxygenation was significantly slowed and incomplete when sulfide was present. A sulfide-mediated decrease in oxygen consumption rate, a shift in intracellular pH or the conversion of hemoglobin to an unusual derivative could all slow in situ hemoglobin deoxygenation. However, under low sulfide levels at which deoxygenation is incomplete, oxygen consumption rate was not inhibited, intracellular pH decreased by less than 0.1 units and the only hemoglobin derivatives present were deoxyhemoglobin and oxyhemoglobin. These results and preliminary measurements of the isolated gill hemoglobin dissociation rate constants suggest that sulfide or a rapidly formed oxidation product may directly influence the rate of Solemya reidi gill hemoglobin deoxygenation.

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