Structure and expression of complex I in plant mitochondria

Grohmann, Lutz; Herz, Udo; Thieck, Oliver; Heiser, Volker; Schmidt-Bleek, K.; Lin, Tse‐I; Brennicke, Axel

doi:10.1016/b978-0-444-82235-2.50036-9

Cited by 2 publications

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“…Plant mitochondrial genomes are much larger in size and appear to contain two more genes coding for complex I subunits (the homologues of the nuclear-encoded bovine 49-kDa and 30-kDa proteins; Oda et al, 1992: Lamattina et al, 1993Gabler et al, 1994;. However, all putative iron-sulfur proteins of the plant complex I are, as in mammals and fungi, encoded by nuclear genes and show a high degree of sequence conservation in their primary structures, in particular of the cysteine-rich sequence stretches which are proposed as the FeS-cluster binding sites (Grohmann et al, 1995). The results of the EPR analysis on the content and characteristics of the iron-sulfur centers thus coincide with our current picture that the plant mitochondrial complex I appears to be structurally and functionally similar to the mammalian and in particular to the fungal counterpart.…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Iron‐Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria

Lin

Sled

Ohnishi

et al. 1995

European Journal of Biochemistry

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The mitochondrial complex I (NADH : ubiquinone oxidoreductase) isolated from potato (Solanum tuberosum) has been investigated for the presence of iron-sulfur clusters. EPR spectroscopic analysis detected signals arising from clusters N1, N2, N3 and N4. Quantitation of the content of iron and sulfur within the isolated complex I showed the preparation to contain 22.6 mol acid-labile sulfide and 30.4 mol irodmol complex I. The iron-sulfur cluster composition of the plant complex I appears to be similar to the well-known composition found in Neurospora crassa.

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Section: Discussionmentioning

confidence: 99%

Analysis of the Iron‐Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria

Lin

Sled

Ohnishi

et al. 1995

European Journal of Biochemistry

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Physiological, biochemical and molecular aspects of mitochondrial complex I in plants

Rasmusson

Heiser

Zabaleta

et al. 1998

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Respiratory complex I of plant mitochondria has to date been investigated with respect to physiological function, biochemical properties and molecular structure. In the respiratory chain complex I is the major entry gate for low potential electrons from matrix NADH, reducing ubiquinone and utilizing the released energy to pump protons across the inner membrane. Plant complex I is active against a background of several other NAD(P)H dehydrogenases, which do not contribute in proton pumping, but permit and establish several different routes of shuttling electrons from NAD(P)H to ubiquinone. Identification of the corresponding molecular structures, that is the proteins and genes of the different NADH dehydrogenases, will allow more detailed studies of this interactive regulatory network in plant mitochondria. Present knowledge of the structure of complex I and the respective mitochondrial and nuclear genes encoding various subunits of this complex in plants is summarized here. Copyright 1998 Elsevier Science B.V.

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Structure and expression of complex I in plant mitochondria

Cited by 2 publications

References 20 publications

Analysis of the Iron‐Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria

Analysis of the Iron‐Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria

Physiological, biochemical and molecular aspects of mitochondrial complex I in plants

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