NADH dehydrogenase


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NADH de·hy·dro·gen·ase

an iron-sulfur-containing flavoprotein reversibly oxidizing NADH to NAD+; an inherited deficiency of this complex results in overwhelming acidosis.

NADH de·hy·dro·gen·ase

(dē-hī'drŏ-jen-ās)
An iron-sulfur-containing flavoprotein reversibly oxidizing NADH to NAD+; an inherited deficiency of this complex results in overwhelming acidosis.
References in periodicals archive ?
In the bovine heart mitochondrial preparations the authors demonstrated that a Dox dose of 25-50 [mu] moles represents the oxidative damage and as they cited this appears to be localized between the NADH dehydrogenase flavin and iron-sulphur center N-1, SDH and cytochrome (oxidase activities) where these two enzymatic activities were shown by Dox by the above authors.
Coenzyme Q10 is a naturally occurring hydrophobic substance that is involved in electron transfer across the mitochondrial membrane from the NADH dehydrogenase complex and the succinate-Q reductase complex to cytochrome c (Cephalalgia 2002;22:137-41).
NADH dehydrogenase activity was measured with a spectrophotometer (Lambda 3B uv/vis, Perkin-Elmer Corporation, Norwalk, CT) at 25 [degrees] C.
Through the selection pressure analysis of 13 PCGs, positive sites were detected in four genes, of which three were NADH dehydrogenase genes and one was Cytochrome c oxidase gene.
Mitochondrial DNA NADH dehydrogenase subunit 2 (ND2) gene were applied to assess genetic variation among eight populations collected from northern to southern part of China coast.
Another shortcoming is that the authors describe the variant as being located in the tRNA (Glu) gene on the one hand and on the other hand as being located in the mitochondrial NADH dehydrogenase subunit 6gene.
LHON is caused by mitochondrial DNA mutations in subunits of NADH dehydrogenase (complex I), leading to reduced oxidative phosphorylation and energy production in retinal cells, resulting in progressive vision loss.
Eight commonly used reference genes were selected in this study (Table 1): NADH dehydrogenase subunit 4 (nd4), gapdh, cox1, rps27, tif5a, rps4, act, and 18S.
Among the identified proteins, we observed decreases in the expression of phospholipid hydroperoxide glutathione peroxidase (PHGPX); ATP synthase subunit O, mitochondrial (ATP5O); glutathione S-transferase Mu 5 (GSTM5), mitochondrial NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10 (NDUFA10).
One of the most studied possible molecular targets for biguanides action is their inhibitory action on respiratory chain complex I (NADH dehydrogenase, NDH), first described in liver tissue [8, 22].
The results suggest that the ndhG (NADH dehydrogenase subunit 6) evolved under positive selection in the C.
Some working groups have focused their analysis on the regions of mitochondrial cytochrome regions of COI and NADH dehydrogenase 1 (ND1) of the parasite as genetic markers (Bowles et al., 1993; Bowles et al., 1994; Bowles et al., 1995; Zhang et al., 1998a; Snabel et al.) based on the sequencing of the mitochondrial DNA and highlighting its importance in the differentiation and discrimination of organisms from the same family, as in the case of Echinococcus strains, which seem to be evolutionary units of high homogeneity (Bowles & McManus, 1993a; Bowles et al., 1993b; Bowles et al, 1992).