Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference55 articles.
1. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain
2. The bacterial energy-transducing NADH-quinone oxidoreductases
3. The Gene Locus of the Proton-translocating NADH : Ubiquinone Oxidoreductase in Escherichia coli
4. Identification of five Rhodobacter capsulatus genes encoding the equivalent of ND subunits of the mitochondrial NADH-ubiquinone oxidoreductase
5. The Proton-translocating NADH-Quinone Oxidoreductase (NDH-1) of Thermophilic Bacterium Thermus thermophilus HB-8
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1. Using a chimeric respiratory chain and EPR spectroscopy to determine the origin of semiquinone species previously assigned to mitochondrial complex I;BMC Biology;2020-05-20
2. Balanced internal hydration discriminates substrate binding to respiratory complex I;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2019-07
3. Balanced internal hydration discriminates substrate binding to respiratory complex I;2019-03-09
4. Chinese mitten crab (Eriocheir sinensis) iron-sulphur cluster assembly protein 2 (EsIscA2) is differentially regulated after immune and oxidative stress challenges;Developmental & Comparative Immunology;2018-07
5. Roles of semiquinone species in proton pumping mechanism by complex I;Journal of Bioenergetics and Biomembranes;2014-07-31
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