PMID: 2117469Jun 12, 1990Paper

Identification of the NADH-binding subunit of NADH-ubiquinone oxidoreductase of Paracoccus denitrificans

Biochemistry
T Yagi, T M Dinh

Abstract

The NADH dehydrogenase complex isolated from Paracoccus denitrificans is composed of approximately 10 unlike polypeptides and contains noncovalently bound FMN, non-heme iron, and acid-labile sulfide [Yagi, T. (1986) Arch. Biochem. Biophys. 250, 302-311]. When the Paracoccus NADH dehydrogenase complex was irradiated by UV light in the presence of [adenylate-32P]NAD, radioactivity was incorporated exclusively into one of three polypeptides of Mr approximately 50,000. Similar results were obtained when [adenylate-32P]NADH was used. The labeling of the Mr 50,000 polypeptide was diminished when UV irradiation of the enzyme with [adenylate-32P]NAD was performed in the presence of NADH, but not in the presence of NADP(H). The labeled polypeptide was isolated by preparative sodium dodecyl sulfate gel electrophoresis and was shown to cross-react with antiserum to the NADH-binding subunit (Mr = 51,000) of bovine NADH-ubiquinone oxidoreductase. Its amino acid composition was also very similar to that of the bovine NADH-binding subunit. These chemical and immunological results indicate that the Mr 50,000 polypeptide is an NADH-binding subunit of the Paracoccus NADH dehydrogenase complex.

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Citations

Apr 1, 1991·Journal of Bioenergetics and Biomembranes·T Yagi
Oct 1, 1991·Journal of Bioenergetics and Biomembranes·H Weiss, T Friedrich
Jun 19, 1998·Biochimica Et Biophysica Acta·T YagiA Matsuno-Yagi
Aug 13, 2011·The Journal of Biological Chemistry·Jesus Torres-BaceteTakao Yagi
Jun 8, 2006·Annual Review of Biochemistry·Ulrich Brandt
Jun 30, 2014·Journal of Bioenergetics and Biomembranes·Motoaki SatoTakao Yagi
Jul 17, 1992·Biochimica Et Biophysica Acta·T YagiA Matsuno-Yagi
Jul 4, 1997·Biochimica Et Biophysica Acta·T V Zharova, A D Vinogradov
Feb 8, 1993·Biochimica Et Biophysica Acta·T Yagi

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