Higher Plant Cell Respiration 1985
DOI: 10.1007/978-3-642-70101-6_6
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The Outer Membrane of Plant Mitochondria

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Cited by 8 publications
(11 citation statements)
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“…Dominant polypeptides of 30, 31, 33, 34, 47, 48 and 74 kDa are strongly enriched in the outer membrane fraction. The presence of strong bands at 30-35 and 45-50 kDa is similar to what has been reported for the outer membrane of Neurospora crassa [23,24], yeast [25] and mung bean cotyledons [8].…”
Section: Resultssupporting
confidence: 86%
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“…Dominant polypeptides of 30, 31, 33, 34, 47, 48 and 74 kDa are strongly enriched in the outer membrane fraction. The presence of strong bands at 30-35 and 45-50 kDa is similar to what has been reported for the outer membrane of Neurospora crassa [23,24], yeast [25] and mung bean cotyledons [8].…”
Section: Resultssupporting
confidence: 86%
“…This protein kinase(s) is Ca2'-dependent since the phosphorylation of histones is abolished in the presence of EGTA (results not shown). The kinase is most likely located on the outer surface of the outer membrane since histones are too large to pass the outer membrane which is impermeable to molecules larger than 5-10 kDa [8]. Consistent with this conclusion, total incorporation is most enhanced by histones in the outer membrane fraction (Table II).…”
Section: Resultssupporting
confidence: 61%
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“…The NAD(P)H dehydrogenase facing the p-side of the inner membrane is known as the externa1 NAD(P)H dehydrogenase (M0ller and Lin, 1986). It can oxidize both NADH and NADPH generated in the cytosol, given the permeability of the outer mitochondrial membrane to molecules up to 3 kD in size (Douce, 1985;Mannella, 1985).Both of these dehydrogenases donate electrons directly to the ubiquinone pool. However, neither catalyzes the translocation of protons across the inner mitochondrial membrane, so the free energy released during electron transfer between NAD(P)H and ubiquinone (73 kJ/2e-) through the activity of either dehydrogenase is lost as heat and not used for ATP synthesis.…”
mentioning
confidence: 99%