Difference between revisions of "Klingenberg 1970 Eur J Biochem"
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|year=1970 | |year=1970 | ||
|journal=Eur J Biochem | |journal=Eur J Biochem | ||
|abstract=Evidence for the localization of the mitochondrial glycerol-phosphate dehydrogenase in the outer phase of the inner membrane is presented. | |abstract=Evidence for the localization of the [[Glycerophosphate dehydrogenase complex |mitochondrial glycerol-phosphate dehydrogenase]] in the outer phase of the inner membrane is presented. | ||
# Glycerol-phosphate does not permeate through the inner membrane to the matrix space in a number of mitochondria which actively oxidize glycerol-phosphate. | # Glycerol-phosphate does not permeate through the inner membrane to the matrix space in a number of mitochondria which actively oxidize glycerol-phosphate. | ||
# The impermeability of the inner membrane to ferricyanide is demonstrated and this forms a basis for elucidating membrane localization of carriers. | # The impermeability of the inner membrane to ferricyanide is demonstrated and this forms a basis for elucidating membrane localization of carriers. |
Revision as of 09:34, 14 December 2014
Klingenberg M (1970) Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane. Eur J Biochem 13:247-52. |
Β» PMID: 5439930
Klingenberg M (1970) Eur J Biochem
Abstract: Evidence for the localization of the mitochondrial glycerol-phosphate dehydrogenase in the outer phase of the inner membrane is presented.
- Glycerol-phosphate does not permeate through the inner membrane to the matrix space in a number of mitochondria which actively oxidize glycerol-phosphate.
- The impermeability of the inner membrane to ferricyanide is demonstrated and this forms a basis for elucidating membrane localization of carriers.
- In mitochondria from various tissues ferricyanide can interact directly with glycerolphosphate dehydrogenase but not with succinate dehydrogenase.
- The oxidation of glycerol-phosphate, in contrast to that of succinate, is insensitive to substrate depletion brought about by uncouplers.
- The results are interpreted to show that both the substrate and the acceptor-site of glycerol-phosphate dehydrogenase are exposed to the outer side of the inner membrane. Thus, for the operation of the glycerol-phosphate dehydrogenase, mitochondria do not require translocases for glycerol-phosphate and dihydroxyacetone-phosphate.
Labels: MiParea: Respiration
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
Regulation: Uncoupler
Coupling state: ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property.
Glycerol-phosphate dehydrogenase, Uncoupler