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Expression of the 25-kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans.
Yano T, Sled VD, Ohnishi T, Yagi T. Yano T, et al. Among authors: ohnishi t. Biochemistry. 1994 Jan 18;33(2):494-9. doi: 10.1021/bi00168a014. Biochemistry. 1994. PMID: 8286379
The energy-transducing NADH-ubiquinone (Q) oxidoreductase of Paracoccus denitrificans is composed of 14 dissimilar subunits and contains at least four iron-sulfur clusters [Yagi, T. (1993) Biochim. Biophys. Acta 1141, 1-17]. The complete DNA sequence of the gene cluster en …
The energy-transducing NADH-ubiquinone (Q) oxidoreductase of Paracoccus denitrificans is composed of 14 dissimilar subunits and contains at …
Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans.
Yano T, Yagi T, Sled VD, Ohnishi T. Yano T, et al. Among authors: ohnishi t. J Biol Chem. 1995 Aug 4;270(31):18264-70. doi: 10.1074/jbc.270.31.18264. J Biol Chem. 1995. PMID: 7629145 Free article.
Previously, we have reported that the NQO2 (25 kDa) subunit was overexpressed as a water-soluble protein in Escherichia coli and was found to ligate a single [2Fe-2S] cluster with rhombic symmetry (gx,y,z = 1.92, 1.95, and 2.00) (Yano, T., Sled', V.D., Ohnishi, T
Previously, we have reported that the NQO2 (25 kDa) subunit was overexpressed as a water-soluble protein in Escherichia coli and was found t …
Conserved nonliganding residues of the Rhodobacter capsulatus Rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool.
Liebl U, Sled V, Brasseur G, Ohnishi T, Daldal F. Liebl U, et al. Among authors: ohnishi t. Biochemistry. 1997 Sep 30;36(39):11675-84. doi: 10.1021/bi970776l. Biochemistry. 1997. PMID: 9305957
Earlier work indicated that in Rhodobacter capsulatus these atoms are provided by two cysteine (C133 and C153) and two histidine (H135 and H156) residues, located at the carboxyl-terminal end of the protein [Davidson, E., Ohnishi, T., Atta-Asafo-Adjei, E., & Dal …
Earlier work indicated that in Rhodobacter capsulatus these atoms are provided by two cysteine (C133 and C153) and two histidine (H135 and H …
The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex.
Brasseur G, Sled V, Liebl U, Ohnishi T, Daldal F. Brasseur G, et al. Among authors: ohnishi t. Biochemistry. 1997 Sep 30;36(39):11685-96. doi: 10.1021/bi970777d. Biochemistry. 1997. PMID: 9305958
In the preceding paper [Liebl, U., Sled, V., Brasseur, G., Ohnishi, T., & Daldal, F. (1997) Biochemistry 36, 11675-11684], the effects of mutations at two of the nonliganding residues [threonine (T) 134 and leucine (L) 136 in the Rhodobactercapsulatus Rie …
In the preceding paper [Liebl, U., Sled, V., Brasseur, G., Ohnishi, T., & Daldal, F. (1997) Biochemistry 36, 11675-11684], …
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