Kraus 1996 J Exp Biol: Difference between revisions
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|authors=Kraus DW, Doeller JE, Powell CS | |authors=Kraus DW, Doeller JE, Powell CS | ||
|year=1996 | |year=1996 | ||
|journal=J | |journal=J Exp Biol | ||
|abstract=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. | |abstract=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. | ||
|mipnetlab=US AL Birmingham Kraus DW | |mipnetlab=US AL Birmingham Kraus DW | ||
| Line 13: | Line 13: | ||
|organism=Plant, Bacteria | |organism=Plant, Bacteria | ||
|kinetics=Reduced Substrate; Cytochrome c, pH | |kinetics=Reduced Substrate; Cytochrome c, pH | ||
|additional=Environmental Physiology; Toxicology | |additional=Environmental Physiology; Toxicology | ||
|discipline=Mitochondrial Physiology | |discipline=Mitochondrial Physiology | ||
}} | }} | ||
Revision as of 18:27, 7 November 2012
| Kraus DW, Doeller JE, Powell CS (1996) Sulfide may directly modify cytoplasmic hemoglobin deoxygenation in Solemya reidi gills. J Exp Biol 199: 1343-1352. |
Kraus DW, Doeller JE, Powell CS (1996) J Exp Biol
Abstract: 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.
• O2k-Network Lab: US AL Birmingham Kraus DW
Labels:
Organism: Plant"Plant" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property., Bacteria"Bacteria" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
HRR: Oxygraph-2k
Environmental Physiology; Toxicology
