Difference between revisions of "Kraus 1996 J Exp Biol"
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|authors=Kraus DW, Doeller JE, Powell CS | |authors=Kraus DW, Doeller JE, Powell CS | ||
|year=1996 | |year=1996 | ||
|journal=J. Exp. Biol. | |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. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/9319227 PMID: 9319227] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/9319227 PMID: 9319227] | ||
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|topics=Respiration; OXPHOS; ETS Capacity | |topics=Respiration; OXPHOS; ETS Capacity | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Revision as of 14:53, 19 October 2010
| 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.
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.
Regulation: Respiration; OXPHOS; ETS Capacity"Respiration; OXPHOS; ETS Capacity" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
HRR: Oxygraph-2k
