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Gene Review

ndh  -  NADH dehydrogenase

Escherichia coli O157:H7 str. EDL933

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Disease relevance of ndh

  • The yjlD (renamed ndh) gene of Bacillus subtilis is predicted to encode an enzyme similar to the NADH dehydrogenase II of Escherichia coli, encoded by the ndh gene [1].
  • The structure of the multifunctional NAD(P)H dehydrogenase type 1 (NDH-1) complexes from cyanobacteria was investigated by growing the wild type and specific ndh His-tag mutants of Thermosynechococcus elongatus BP-1 under different CO(2) conditions, followed by an electron microscopy (EM) analysis of their purified membrane protein complexes [2].

High impact information on ndh

  • Footprint studies indicated that FNR proteins lacking essential cysteine residues are impaired in their ability to protect FNR sites in the ndh promoter [3].
  • The ndh gene regulates expression of the yjlC-ndh operon, as indicated by the fact that mutation in ndh causes a higher NADH/NAD(+) ratio [1].
  • NADH dehydrogenase-2 (NDH-2) from Escherichia coli respiratory chain is a membrane-bound cupric-reductase encoded by ndh gene [4].
  • A mutant strain complemented with ndh gene almost recovered the parental phenotype for growing in copper limitation or excess [4].
  • Here, we report that the respiratory system of a ndh deficient strain suffered a faster inactivation than that of the parental strain in the presence of tert-butyl hydroperoxide due to endogenous copper [4].

Anatomical context of ndh


  1. Regulatory Loop between Redox Sensing of the NADH/NAD+ Ratio by Rex (YdiH) and Oxidation of NADH by NADH Dehydrogenase Ndh in Bacillus subtilis. Gyan, S., Shiohira, Y., Sato, I., Takeuchi, M., Sato, T. J. Bacteriol. (2006) [Pubmed]
  2. Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy. Arteni, A.A., Zhang, P., Battchikova, N., Ogawa, T., Aro, E.M., Boekema, E.J. Biochim. Biophys. Acta (2006) [Pubmed]
  3. Properties of FNR proteins substituted at each of the five cysteine residues. Green, J., Sharrocks, A.D., Green, B., Geisow, M., Guest, J.R. Mol. Microbiol. (1993) [Pubmed]
  4. The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the bacterial growth in extreme copper concentrations and increases the resistance to the damage caused by copper and hydroperoxide. Rodríguez-Montelongo, L., Volentini, S.I., Farías, R.N., Massa, E.M., Rapisarda, V.A. Arch. Biochem. Biophys. (2006) [Pubmed]
  5. Superoxide production by respiring membranes of Escherichia coli. Imlay, J.A., Fridovich, I. Free Radic. Res. Commun. (1991) [Pubmed]
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