The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria

Carneiro, Patrı́cia; Duarte, Margarida; Videira, Arnaldo

doi:10.1016/j.bbabio.2003.10.004

Cited by 37 publications

(42 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…NDH-2 of E. coli contains the predicted transmembrane domain at the C-terminal region, 19) and the external alternative NADH dehydrogenase of N. crassa also contains a transmembrane domain at the N-terminal region. 35) On the other hand, NDH-2 of A. ambivalens contains 3 possible putative amphipatic helices located around amino acid residues 15-27, 181-194 and 332-347, which are also present in E. coli NDH-2.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Electron Transfer Ability from NADH to Menaquinone and from NADPH to Oxygen of Type II NADH Dehydrogenase ofCorynebacterium glutamicum

Nantapong

Otofuji

Migita

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

“…The external alternative NADH dehydrogenases NDE-1 and NDE-2 of N. crassa oxidize NADPH at acidic pH, similarly to the C. glutamicum enzyme. 35,37) Therefore, a phylogenetic tree of NDH-2 from various organisms including C. glutamicum was constructed using the Clustal W program (Fig. 7).…”

Section: Discussionmentioning

confidence: 99%

Electron Transfer Ability from NADH to Menaquinone and from NADPH to Oxygen of Type II NADH Dehydrogenase ofCorynebacterium glutamicum

Nantapong

Otofuji

Migita

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

“…5B). Such a pattern of activity has already been described for other NADHdependent NDH-2 enzymes (35,39,40). Catalytic properties of Nda2 were determined at optimal pH by using NADH or NADPH as electron donors and Qo as an acceptor ( Table 1).…”

Section: Six C Reinhardtii Genes Encode For Putative Type Ii Nadhmentioning

confidence: 99%

Characterization of Nda2, a Plastoquinone-reducing Type II NAD(P)H Dehydrogenase in Chlamydomonas Chloroplasts

Desplats¹,

Mus²,

Cuiné

et al. 2009

Journal of Biological Chemistry

145

100

View full text Add to dashboard Cite

Electron transfer pathways associated to oxygenic photosynthesis, including cyclic electron flow around photosystem I and chlororespiration, rely on non-photochemical reduction of plastoquinones (PQs). In higher plant chloroplasts, a bacteriallike NDH complex homologous to complex I is involved in PQ reduction, but such a complex is absent from Chlamydomonas plastids where a type II NAD(P)H dehydrogenase activity has been proposed to operate. With the aim to elucidate the nature of the enzyme-supporting non-photochemical reduction of PQs, one of the type II NAD(P)H dehydrogenases identified in the Chlamydomonas reinhardtii genome (Nda2) was produced as a recombinant protein in Escherichia coli and further characterized. As many type II NAD(P)H dehydrogenases, Nda2 uses NADH as a preferential substrate, but in contrast to the eukaryotic enzymes described so far, contains non-covalently bound FMN as a cofactor. When expressed at a low level, Nda2 complements growth of an E. coli lacking both NDH-1 and NDH-2, but is toxic at high expression levels. Using an antibody raised against the recombinant protein and based on its mass spectrometric identification, we show that Nda2 is localized in thylakoid membranes. Chlorophyll fluorescence measurements performed on thylakoid membranes show that Nda2 is able to interact with thylakoid membranes of C. reinhardtii by reducing PQs from exogenous NADH or NADPH. We discuss the possible involvement of Nda2 in cyclic electron flow around PSI, chlororespiration, and hydrogen production.

show abstract

“…With the release of the N. crassa genome (22), at least two other sequences encoding putative NDH-2 dehydrogenases were identified. These proteins have recently been characterized; one corresponds to NDE2 (11), and the other was identified as the internal rotenone-insensitive NADH dehydrogenase (NDI1) (17).…”

Section: Biochemical and Genomic Aspects Of Nad(p)h Dehydrogenasesmentioning

confidence: 99%

New Insights into Type II NAD(P)H:Quinone Oxidoreductases

Melo

Bandeiras

Teixeira

2004

Microbiol Mol Biol Rev

238

212

View full text Add to dashboard Cite

Type II NAD(P)H:quinone oxidoreductases (NDH-2) catalyze the two-electron transfer from NAD(P)H to quinones, without any energy-transducing site. NDH-2 accomplish the turnover of NAD(P)H, regenerating the NAD(P)+ pool, and may contribute to the generation of a membrane potential through complexes III and IV. These enzymes are usually constituted by a nontransmembrane polypeptide chain of ∼50 kDa, containing a flavin moiety. There are a few compounds that can prevent their activity, but so far no general specific inhibitor has been assigned to these enzymes. However, they have the common feature of being resistant to the complex I classical inhibitors rotenone, capsaicin, and piericidin A. NDH-2 have particular relevance in yeasts like Saccharomyces cerevisiae and in several prokaryotes, whose respiratory chains are devoid of complex I, in which NDH-2 keep the [NADH]/[NAD+] balance and are the main entry point of electrons into the respiratory chains. Our knowledge of these proteins has expanded in the past decade, as a result of contributions at the biochemical level and the sequencing of the genomes from several organisms. The latter showed that most organisms contain genes that potentially encode NDH-2. An overview of this development is presented, with special emphasis on microbial enzymes and on the identification of three subfamilies of NDH-2

show abstract

The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria

Cited by 37 publications

References 43 publications

Electron Transfer Ability from NADH to Menaquinone and from NADPH to Oxygen of Type II NADH Dehydrogenase ofCorynebacterium glutamicum

Electron Transfer Ability from NADH to Menaquinone and from NADPH to Oxygen of Type II NADH Dehydrogenase ofCorynebacterium glutamicum

Characterization of Nda2, a Plastoquinone-reducing Type II NAD(P)H Dehydrogenase in Chlamydomonas Chloroplasts

New Insights into Type II NAD(P)H:Quinone Oxidoreductases

Contact Info

Product

Resources

About