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Gene Review:

TTC0057 - NADH dehydrogenase

Thermus thermophilus HB27

Yagi, T. et al., Yagi, T. et al., Cava, F. et al.

Yagi, Seo, Di Bernardo, Nakamaru-Ogiso, Kao, Matsuno-Yagi,

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Disease relevance of TTC0057

A new type of NADH dehydrogenase specific for nitrate respiration in the extreme thermophile Thermus thermophilus [1].
The activities of both NADH dehydrogenases were stable at temperatures of greater than or equal to 80 degrees C. The occurrence of two distinct types of NADH dehydrogenase as a common feature in the membranes of various aerobic bacteria is discussed [2].
Recently, the study of the NADH dehydrogenase complex has taken on new urgency as a result of reports that complex I defects are involved in many human mitochondrial diseases [3].

High impact information on TTC0057

The purified NADH dehydrogenase 1 contained noncovalently bound FMN, non-heme iron, and acid-labile sulfide [2].
The purified NADH dehydrogenase 2 contained noncovalently bound FAD and no non-heme iron or acid-labile sulfide [2].
This review article is concerned with two on-going research projects in our laboratory, both of which are related to the study of the NADH dehydrogenase enzyme complexes in the respiratory chain [3].

References

A new type of NADH dehydrogenase specific for nitrate respiration in the extreme thermophile Thermus thermophilus. Cava, F., Zafra, O., Magalon, A., Blasco, F., Berenguer, J. J. Biol. Chem. (2004) [Pubmed]
Purification and characterization of two types of NADH-quinone reductase from Thermus thermophilus HB-8. Yagi, T., Hon-nami, K., Ohnishi, T. Biochemistry (1988) [Pubmed]
NADH dehydrogenases: from basic science to biomedicine. Yagi, T., Seo, B.B., Di Bernardo, S., Nakamaru-Ogiso, E., Kao, M.C., Matsuno-Yagi, A. J. Bioenerg. Biomembr. (2001) [Pubmed]

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