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The effects of cadmium on succinate and NADH‐linked substrate oxidations in rat hepatic mitochondria
Author(s) -
Cameron I.,
McNamee P. M.,
Markham A.,
Morgan R. M.,
Wood M.
Publication year - 1986
Publication title -
journal of applied toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.784
H-Index - 87
eISSN - 1099-1263
pISSN - 0260-437X
DOI - 10.1002/jat.2550060505
Subject(s) - oligomycin , respiration , nad+ kinase , mitochondrion , ferricyanide , cadmium , rotenone , biochemistry , succinate dehydrogenase , chemistry , enzyme , dehydrogenase , atpase , submitochondrial particle , biology , organic chemistry , botany
Low concentrations of cadmium (3.3–40 μ M ) inhibited State 3 NADH‐linked respiration in rat hepatic mitochondria, but failed to release oligomycin (1 μ M ) inhibited State 3 respiration, or to significantly change the State 4 rate. In the presence of succinate, (40 μ M ) cadmium inhibited State 3 respiration by 89%, while concentrations between 3.3 and (13.3 μ M ) stimulated State 4 respiration. Higher concentrations caused marked inhibition. In the presence of succinate, cadmium released oligomycin inhibited State 3 respiration. Cadmium (0.001–1.0 m M ) did not stimulate mitochondrial ATPase activity or inhibit ferricyanide reduction, but stimulated NAD + linked mitochondrial dehydrogenase activities and NADH oxidation. These results indicate that cadmium interacts with either the NADH dehydrogenase complex or other NADH‐dependent enzymes and solely by an uncompling action.