Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [<sup>3</sup>H]dihydrorotenone

Earley, Fergus G.P.; Patel, S.; Ragan, C I; Attardi, Giuseppe

doi:10.1016/0014-5793(87)81200-0

Cited by 189 publications

(103 citation statements)

References 18 publications

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“…34 complete sequences from mitochondrial, plastidial and bacterial species were taken from recent versions of the EMBL data banks and aligned as in [19]. The average hydropathy and amphipathy profile of the aligned sequences confirmed the analysis in [20] except that the region corresponding to the previously proposed helix H [20] was not predicted to be transmembranous.…”

Section: Methodsmentioning

confidence: 76%

“…Previously, the binding of a radiolabelled analog of rotenone was associated to another subunit of the complex, namely ND 1 [20]. However, rotenone binds to complex I in a complicated way, because two binding sites are present and several subunits could form such a binding site (see [13,21] and references therein).…”

Section: Relationship Between Structure and Function Of The Nd4 Subunitmentioning

confidence: 99%

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Functional alterations of the mitochondrially encoded ND4 subunit associated with Leber's hereditary optic neuropathy

et al. 1994

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Leber's hereditary optic neuropathy (LHON) is a maternally inherited disease associated with point mutations in mitochondrial DNA. The most frequent of these mutations is the G-to-A substitution at nucleotide position 11,778 which changes an evolutionarily conserved arginine with a histidine at position 340 in subunit ND4 of NADH : ubiquinone reductase (respiratory complex I). We report that this amino acid substitution alters the affinity of complex I for the ubiquinone substrate and induces resistance towards its potent inhibitor rotenone in mitochondria of LHON patients. Such changes could reflect a substantial loss in the energy conserving function of NADH: ubiquinone reductase and thus explain the pathological effect of the ND4/11,778 mutation.

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Section: Methodsmentioning

confidence: 76%

Section: Relationship Between Structure and Function Of The Nd4 Subunitmentioning

confidence: 99%

Functional alterations of the mitochondrially encoded ND4 subunit associated with Leber's hereditary optic neuropathy

et al. 1994

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“…It comprises at least 30 different subunits, most of which are encoded by nuclear genes and imported from the cytoplasm. Despite the fact that in many organisms the primary structure of the mitochondrial DNA-encoded subunits has been determined, little is known about their functions, with the exception of the ND1 subunit, which is known to bind rotenone (Earley et al, 1987) and interact with ubiquinone (Friedrich et al, 1990). …”

Section: Discussionmentioning

confidence: 99%

Alteration of Dark Respiration and Reduction of Phototrophic Growth in a Mitochondrial DNA Deletion Mutant of Chlamydomonas Lacking cob, nd4, and the 3′ End of nd5

Duby

Matagne

1999

Plant Cell

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We describe here a new type of mitochondrial mutation ( dum24 ; for dark uniparental minus inheritance) of the unicellular photosynthetic alga Chlamydomonas reinhardtii . The mutant fails to grow under heterotrophic conditions and displays reduced growth under both photoautotrophic and mixotrophic conditions. In reciprocal crosses between mutant and wild-type cells, the meiotic progeny only inherit the phenotype of the mating-type minus parent, indicating that the dum24 mutation exclusively affects the mitochondrial genome. Digestion with various restriction enzymes followed by DNA gel blot hybridizations with specific probes demonstrated that dum24 cells contain four types of altered mitochondrial genomes: deleted monomers lacking cob , nd4 , and the 3 Ј end of the nd5 gene; deleted monomers deprived of cob , nd4 , nd5 , and the 5 Ј end of the cox1 coding sequence; and two types of dimers produced by end-to-end fusions between monomers similarly or differently deleted. Due to these mitochondrial DNA alterations, complex I activity, the cytochrome pathway of respiration, and presumably, the three phosphorylation sites associated with these enzyme activities are lacking in the mutant. The low respiratory rate of the dum24 cells results from the activities of rotenoneresistant NADH dehydrogenase, complex II, and alternative oxidase, with none of these enzymes being coupled to ATP production. To our knowledge, this type of mitochondrial mutation has never been described for photosynthetic organisms or more generally for obligate aerobes.

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“…The labelling was not affected by the complete inhibition by rotenone, although the ND1 subunit can bind this inhibitor as well (Earley and Ragan 1984;Earley et al 1987). Also piericidin A can bind to ND1 (Murai et al 2007).…”

Section: >200 Msmentioning

confidence: 99%

“…The NAD(P)H→O 2 and NAD(P)H→K 3 Fe(CN) 6 data are from steady-state experiments. All turnover numbers refer to NAD(P)H consumption and are standardised to 22°C assuming a two-fold change in rate per 10°C the ND1 subunit (Earley and Ragan 1984;Earley et al 1987;Murai et al 2007). It is hypothesised here that also the inhibition by these poisons is primarily due to the blockage of proton transfer, resulting in inhibition of electron transfer.…”

Section: Kinetic Issues Reactions With Nad(p)hmentioning

confidence: 99%

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited

Albracht

2010

J Bioenerg Biomembr

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Bovine NADH:ubiquinone oxidoreductase (Complex I) is the first complex in the mitochondrial respiratory chain. It has long been assumed that it contained only one FMN group. However, as demonstrated in 2003, the intact enzyme contains two FMN groups. The second FMN was proposed to be located in a conserved flavodoxin fold predicted to be present in the PSST subunit. The longknown reaction of Complex I with NADPH differs in many aspects from that with NADH. It was proposed that the second flavin group was specifically involved in the reaction with NADPH. The X-ray structure of the hydrophilic domain of Complex I from Thermus thermophilus (Sazanov and Hinchliffe 2006, Science 311, 1430-1436 disclosed the positions of all redox groups of that enzyme and of the subunits holding them. The PSST subunit indeed contains the predicted flavodoxin fold although it did not contain FMN. Inspired by this structure, the present paper describes a re-evaluation of the enigmatic reactions of the bovine enzyme with NADPH. Published data, as well as new freeze-quench kinetic data presented here, are incompatible with the general opinion that NADPH and NADH react at the same site. Instead, it is proposed that these pyridine nucleotides react at opposite ends of the 90Å long chain of prosthetic groups in Complex I. Ubiquinone is proposed to react with the Fe-S clusters in the TYKY subunit deep inside the hydrophilic domain. A new model for electron transfer in Complex I is proposed. In the accompanying paper this model is compared with the one advocated in current literature.

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Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [³H]dihydrorotenone

Cited by 189 publications

References 18 publications

Functional alterations of the mitochondrially encoded ND4 subunit associated with Leber's hereditary optic neuropathy

Functional alterations of the mitochondrially encoded ND4 subunit associated with Leber's hereditary optic neuropathy

Alteration of Dark Respiration and Reduction of Phototrophic Growth in a Mitochondrial DNA Deletion Mutant of Chlamydomonas Lacking cob, nd4, and the 3′ End of nd5

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited

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Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [3H]dihydrorotenone

Cited by 189 publications

References 18 publications

Functional alterations of the mitochondrially encoded ND4 subunit associated with Leber's hereditary optic neuropathy

Functional alterations of the mitochondrially encoded ND4 subunit associated with Leber's hereditary optic neuropathy

Alteration of Dark Respiration and Reduction of Phototrophic Growth in a Mitochondrial DNA Deletion Mutant of Chlamydomonas Lacking cob, nd4, and the 3′ End of nd5

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited

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Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [³H]dihydrorotenone