Výsledky vyhledávání - "S. W. Meinhardt"

Additional Sources of Resistance to Tan Spot of Wheat

Autor: S. W. Meinhardt, L. J. Francl, James A. Anderson, C. R. Riede, James G. Jordahl

Publikováno v: Crop Science. 36:771-777

Tan spot, a foliar disease of wheat (Triticum aestivum L. em Thell) and durum (T. turgidum var. durum L.) caused by Pyrenophora triticirepentis (Died.) Drechs., reduces yield in susceptible cultivars by 3 to 50%. Additional sources for resistance to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0d57ca1964762d5bd28b94f1ddda21ab
https://doi.org/10.2135/cropsci1996.0011183x003600030040x

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Biophysical and biochemical studies of bacterial NADH:quinone oxidoreductase (NDH-1)

Autor: Tomoko Ohnishi, V. D. Sled', N. I. Rudnitzky, B. W. Jacobson, Y. Fukumori, S. W. Meinhardt, M. W. Calhoun, R. B. Gennis, H. Leif, T. Friedrich, H. Weiss

Publikováno v: Biochemical Society transactions. 22(1)

The mitochondrial NADH-Q oxidoreductase (Complex I) is the most complex among the major mitochondrial energy coupling enzymes. Complex I from bovine heart and Neurosporu crussu contains 41 (1) and >32 (2) distinct subunits, respectively. In contrast,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d39928a81af430ea8c1a630db952f2c
https://pubmed.ncbi.nlm.nih.gov/8206301

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Studies on the NADH-menaquinone oxidoreductase segment of the respiratory chain in Thermus thermophilus HB-8

Autor: S W, Meinhardt, D C, Wang, K, Hon-nami, T, Yagi, T, Oshima, T, Ohnishi

Publikováno v: The Journal of biological chemistry. 265(3)

Five distinct low potential iron-sulfur clusters have been identified potentiometrically in the membrane particles from Thermus thermophilus HB-8. Three of these clusters (designated as [N-1H]T, [N-2H]T, and [N-3]T) exhibit the following midpoint red

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::04de89d201718b94e115e58040d17b1a
https://pubmed.ncbi.nlm.nih.gov/2153129

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Akademický článek

Molecular-based race classification of Pyrenophora tritici-repentis causing tan spot of wheat in Japan.

Autor: Keita Kato¹, Yusuke Ban¹, Mikiko Yanaka², Shoya Kitabayashi¹, Hiroyuki Sekiguchi³, Keisuke Tomioka¹, Miwako Ito¹ miwako@naro.affrc.go.jp

Publikováno v: Breeding Science. 2023, Vol. 73 Issue 5, p445-449. 5p.

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Structure and function of the mitochondrial bc1 complex. A mutational analysis of the yeast Rieske iron-sulfur protein

Autor: D L, Gatti, S W, Meinhardt, T, Ohnishi, A, Tzagoloff

Publikováno v: Journal of molecular biology. 205(2)

Respiratory-defective mutants of Saccharomyces cerevisiae assigned to a single complementation group (G12) have been determined to have lesions in the iron-sulfur protein (Rieske protein) of ubiquinol: cytochrome c reductase. Mutants capable of expre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::015ab72b5892597cda2d0aa7c3913d53
https://pubmed.ncbi.nlm.nih.gov/2538628

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Identification of a stable ubisemiquinone and characterization of the effects of ubiquinone oxidation-reduction status on the Rieske iron-sulfur protein in the three-subunit ubiquinol-cytochrome c oxidoreductase complex of Paracoccus denitrificans

Autor: S W, Meinhardt, X H, Yang, B L, Trumpower, T, Ohnishi

Publikováno v: The Journal of biological chemistry. 262(18)

The ubiquinol-cytochrome c oxidoreductase (cytochrome bc1) complex from Paracoccus denitrificans exhibits a thermodynamically stable ubisemiquinone radical detectable by EPR spectroscopy. The radical is centered at g = 2.004, is sensitive to antimyci

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::96a04d1eb4122d5d5bf8ff0ebab2af14
https://pubmed.ncbi.nlm.nih.gov/3036822

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EPR characterization of the iron-sulfur clusters in the NADH: ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans

Autor: S W, Meinhardt, T, Kula, T, Yagi, T, Lillich, T, Ohnishi

Publikováno v: The Journal of biological chemistry. 262(19)

The physicochemical properties of the iron-sulfur clusters present in the NADH:ubiquinone oxidoreductase of Paracoccus denitrificans have been examined in the cytoplasmic membrane particles by redox potentiometry and EPR spectroscopy. Analogous to th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::15f898a24bd45aaec16c73ca139d85fb
https://pubmed.ncbi.nlm.nih.gov/3036849

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Spatial organization of redox active centers in the bovine heart ubiquinol-cytochrome c oxidoreductase

Autor: T, Ohnishi, H, Schägger, S W, Meinhardt, R, LoBrutto, T A, Link, G, von Jagow

Publikováno v: The Journal of biological chemistry. 264(2)

We have examined the spatial organization of the redox active centers in the Site II segment of the bovine heart respiratory chain by using reconstituted proteoliposomes of ubiquinol-cytochrome c oxidoreductase (Complex III or cytochrome bc1 complex)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::22058a7758399fb894f1fa5e46baa5b5
https://pubmed.ncbi.nlm.nih.gov/2536023

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