The ubiquinone-mediated interaction between the external NADH dehydrogenase and the cytochromes b-c1 complex in plant mitochondria

1981 ◽  
Vol 9 (5) ◽  
pp. 429-429 ◽  
Author(s):  
I. R. COTTINGHAM ◽  
A. L. MOORE
Keyword(s):  
Nadh Dehydrogenase ◽  
Plant Mitochondria

scholarly journals Oxidation and reduction of pyridine nucleotides in alamethicin-permeabilized plant mitochondria

2004 ◽  
Vol 380 (1) ◽  
pp. 193-202 ◽  
Author(s):  
Fredrik I. JOHANSSON ◽  
Agnieszka M. MICHALECKA ◽  
Ian M. MØLLER ◽  
Allan G. RASMUSSON
Keyword(s):  
Electron Transport ◽  
Complex I ◽  
Electron Transport Chain ◽  
Nadh Dehydrogenase ◽  
Plant Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Intact Cells ◽  
Transport Chain ◽  
Invasive Method

The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and metabolites across the membrane. This constitutes a problem when intramitochondrial enzymes are studied. The channel-forming antibiotic AlaM (alamethicin) was used as a potentially less invasive method to permeabilize mitochondria and study the highly branched electron-transport chain in potato tuber (Solanum tuberosum) and pea leaf (Pisum sativum) mitochondria. We show that AlaM permeabilized the inner membrane of plant mitochondria to NAD(P)H, allowing the quantification of internal NAD(P)H dehydrogenases as well as matrix enzymes in situ. AlaM was found to inhibit the electron-transport chain at the external Ca2+-dependent rotenone-insensitive NADH dehydrogenase and around complexes III and IV. Nevertheless, under optimal conditions, especially complex I-mediated NADH oxidation in AlaM-treated mitochondria was much higher than what has been previously measured by other techniques. Our results also show a difference in substrate specificities for complex I in mitochondria as compared with inside-out submitochondrial particles. AlaM facilitated the passage of cofactors to and from the mitochondrial matrix and allowed the determination of NAD+ requirements of malate oxidation in situ. In summary, we conclude that AlaM provides the best method for quantifying NADH dehydrogenase activities and that AlaM will prove to be an important method to study enzymes under conditions that resemble their native environment not only in plant mitochondria but also in other membrane-enclosed compartments, such as intact cells, chloroplasts and peroxisomes.

Titration of the external NADH dehydrogenase and the alternative oxidase in plant mitochondria

1994 ◽  
Vol 22 (4) ◽  
pp. 406S-406S ◽  
Author(s):  
GRAEME R. LEACH ◽  
KLAAS KRAB ◽  
ANTHONY L. MOORE
Keyword(s):  
Nadh Dehydrogenase ◽  
Alternative Oxidase ◽  
Plant Mitochondria

Variable intron content of the NADH dehydrogenase subunit 4 gene of plant mitochondria

1992 ◽  
Vol 21 (4-5) ◽  
pp. 423-430 ◽  
Author(s):  
David A. Gass ◽  
Christopher A. Makaroff ◽  
Jeffrey D. Palmer
Keyword(s):  
Nadh Dehydrogenase ◽  
Plant Mitochondria ◽  
Nadh Dehydrogenase Subunit ◽  
Intron Content

scholarly journals Immunological analysis of plant mitochondrial NADH dehydrogenases

1986 ◽  
Vol 236 (1) ◽  
pp. 201-207 ◽  
Author(s):  
I R Cottingham ◽  
M W J Cleeter ◽  
C I Ragan ◽  
A L Moore
Keyword(s):  
Nadh Dehydrogenase ◽  
Plant Mitochondria ◽  
The Other ◽  
Mitochondrial Inner Membrane ◽  
Crossed Immunoelectrophoresis ◽  
Specific Antisera ◽  
Molecular Masses ◽  
Nadh Dehydrogenases ◽  
Single Polypeptide ◽  
Triton X

Plant mitochondrial NADH dehydrogenases were analysed by two immunological strategies. The first exploited an antiserum raised to a preparation of SDS-solubilized mitochondrial-inner-membrane particles. By using a combination of activity-immunoprecipitation and crossed immunoelectrophoresis, it was shown that Triton X-100-solubilized membranes contain at least three immunologically distinct NADH dehydrogenases. Two of these were subsequently isolated by line immunoelectrophoresis and analysed for polypeptide composition: one contained three polypeptides with molecular masses of 75, 62 and 41 kDa; the other was a single polypeptide with a molecular mass of 53 kDa. The other approach was to probe plant mitochondrial membranes with antibodies raised to a purified preparation of ox heart rotenone-sensitive NADH dehydrogenase and subunits thereof. Cross-reactions were observed with the subunit-specific antisera against the 30 and 49 kDa ox heart proteins. However, the molecular masses of the equivalent polypeptides in plant mitochondria are slightly lower, at 27 and 46 kDa respectively.

scholarly journals The activation of non-phosphorylating electron transport by adenine nucleotides in Jerusalem-artichoke (Helianthus tuberosus) mitochondria

1975 ◽  
Vol 152 (3) ◽  
pp. 637-645 ◽  
Author(s):  
R Sotthibandhu ◽  
J M Palmer
Keyword(s):  
Cytochrome B ◽  
Redox State ◽  
Nadh Dehydrogenase ◽  
Adenine Nucleotides ◽  
Plant Mitochondria ◽  
Jerusalem Artichoke ◽  
Simultaneous Oxidation ◽  
Carbonyl Cyanide ◽  
Bongkrekic Acid ◽  
Complex Manner

In isolated plant mitochondria the oxidation of both succinate and exogenous NADH responded in the expected manner to the addition of ADP or uncoupling agents, and the uncoupled rate of respiration was often in excess of the rate obtained in the presence of ADP. However, the oxidation of NAD+-linked substrates responded in a much more complex manner to the addition of ADP or uncoupling agents such as carbonyl cyanide p-trifluoromethoxyphenylhydrazone to mitochondria oxidizing pyruvate plus malate failed to result in a reliable stimulation; this uncoupled rate could be stimulated by adding AMP or ADP in the presence of oligomycin or bongkrekic acid. Spectrophometric measurements showed that the addition of AMP or ADP resulted in the simultaneous oxidation of endogenous nicotinamide nucleotide and the reduction of cytochrome b. ADP was only effective in bringing about these changes in redox state in the presence of Mg2+ whereas AMP did not require Mg2+. It was concluded that AMP activated the flow of electrons from endogenous nicotinamide nucleotide to cytochrome b, possible at the level of the internal NADH dehydrogenase.

Nitric oxide inhibits succinate dehydrogenase-driven oxygen consumption in potato tuber mitochondria in an oxygen tension-independent manner

2012 ◽  
Vol 449 (1) ◽  
pp. 263-273 ◽  
Author(s):  
Vagner Simonin ◽  
Antonio Galina
Keyword(s):  
Nitric Oxide ◽  
Oxygen Consumption ◽  
Potato Tuber ◽  
Succinate Dehydrogenase ◽  
Mitochondrial Respiration ◽  
Complex I ◽  
Nadh Dehydrogenase ◽  
Electron Flow ◽  
Plant Mitochondria ◽  
Deta Nonoate

NO (nitric oxide) is described as an inhibitor of plant and mammalian respiratory chains owing to its high affinity for COX (cytochrome c oxidase), which hinders the reduction of oxygen to water. In the present study we show that in plant mitochondria NO may interfere with other respiratory complexes as well. We analysed oxygen consumption supported by complex I and/or complex II and/or external NADH dehydrogenase in Percoll-isolated potato tuber (Solanum tuberosum) mitochondria. When mitochondrial respiration was stimulated by succinate, adding the NO donors SNAP (S-nitroso-N-acetyl-DL-penicillamine) or DETA-NONOate caused a 70% reduction in oxygen consumption rate in state 3 (stimulated with 1 mM of ADP). This inhibition was followed by a significant increase in the Km value of SDH (succinate dehydrogenase) for succinate (Km of 0.77±0.19 to 34.3±5.9 mM, in the presence of NO). When mitochondrial respiration was stimulated by external NADH dehydrogenase or complex I, NO had no effect on respiration. NO itself and DETA-NONOate had similar effects to SNAP. No significant inhibition of respiration was observed in the absence of ADP. More importantly, SNAP inhibited PTM (potato tuber mitochondria) respiration independently of oxygen tensions, indicating a different kinetic mechanism from that observed in mammalian mitochondria. We also observed, in an FAD reduction assay, that SNAP blocked the intrinsic SDH electron flow in much the same way as TTFA (thenoyltrifluoroacetone), a non-competitive SDH inhibitor. We suggest that NO inhibits SDH in its ubiquinone site or its Fe–S centres. These data indicate that SDH has an alternative site of NO action in plant mitochondria.

scholarly journals Regulation of malate oxidation in plant mitochondria. Response to rotenone and exogenous NAD+

1982 ◽  
Vol 208 (3) ◽  
pp. 703-711 ◽  
Author(s):  
J M Palmer ◽  
J P Schwitzguébel ◽  
I M Møller
Keyword(s):  
Nadh Dehydrogenase ◽  
Tricarboxylic Acid Cycle ◽  
Plant Mitochondria ◽  
Jerusalem Artichoke ◽  
Atp Synthesis ◽  
Matrix Space ◽  
Matrix Surface ◽  
The Matrix ◽  
Nadh Dehydrogenases ◽  
Malate Oxidation

Exogenous NAD+ stimulated the rotenone-resistant oxidation of all the NAD+-linked tricarboxylic acid-cycle substrates in mitochondria from Jerusalem artichoke (Helianthus tuberosus L.) tubers. The stimulation was not removed by the addition of EGTA, which is known to inhibit the oxidation of exogenous NADH. It is therefore concluded that added NAD+ gains access to the matrix space and stimulates oxidation by the rotenone-resistant NADH dehydrogenase located on the matrix surface of the inner membrane. Added NAD+ stimulated the activity of malic enzyme and displaced the equilibrium of malate dehydrogenase; both observations are consistent with entry of NAD+ into the matrix space. Analysis of products of malate oxidation showed that rotenone-resistant oxygen uptake only occurred when the concentration of oxaloacetate was low and that of NADH was high. Thus it is proposed that the concentration of NADH regulates the activity of the two internal NADH dehydrogenases. Evidence is presented to suggest that the rotenone-resistant NADH dehydrogenase is engaged under conditions of high phosphorylation potential, which restricts electron flux through the rotenone-sensitive dehydrogenase (coupled to ATP synthesis).

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