A four-subunit cytochrome bc1 complex complements the respiratory chain of Thermus thermophilus
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چکیده
منابع مشابه
Studies on cytochrome c oxidase activity of the cytochrome c1aa3 complex from Thermus thermophilus.
Cytochrome oxidase from T. thermophilus is isolated as a noncovalent complex of cytochromes c1 and aa3 in which the four redox components of aa3 appear to be associated with a single approximately 55,000-D subunit while the heme C is associated with a approximately 33,000-D peptide (Yoshida, T., Lorence, R. M., Choc, M. G., Tarr, G. E., Findling, K. L., and Fee, J. A. (1983) J. Biol. Chem. 258,...
متن کاملStudies on Cytochrome c Oxidase Activity of the Cytochrome ~ 1 ctct 3 Complex from Thermus thermophilus
Cytochrome oxidase from T. thermophilus is isolated as a noncovalent complex of cytochromes c1 and aa3 in which the four redox components of aa3 appear to be associated with a single -55,000-D subunit while the heme C is associated with a -33,000-D peptide (Yoshida, T., Lorence, R. M., Choc, M. G., Tarr, G. E., Findling, K. L., and Fee, J. A. (1983) J. Biol. Chem. 258, 112-123). We have examine...
متن کاملCrystallization of cytochrome bc1 complex.
Complex III (cytochrome bc1 particle; ubiquinol:ferricytochrome c oxidoreductase, EC 1.10.2.2) was purified from beef heart mitochondria by a combination of hydrophobic interaction and affinity chromatography. By washing the complex with detergent on the hydrophobic interaction column, phospholipids were effectively depleted; 7 mol of cardiolipin per mol of cytochrome c1 was retained in the fin...
متن کاملPotentiometric study of cytochrome c1aa3 from Thermus thermophilus.
We have examined the redox behavior of the cytochrome c1aa3 complex from Thermus thermophilus. In potentiometric titrations the cytochrome c behaves as an independent center having n = 1 and E = 205 mV (NHE). Under the assumption that the individual centers equilibrate independently in this experiment, changes in the absorption band at 603 nm have been resolved into two components: cytochrome a...
متن کاملStructure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.
Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contai...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2005
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2005.03.008