Interaction of Cytochrome C Oxidase with Steroid Hormones
Estradiol, testosterone and other steroid hormones inhibit cytochrome <i>c</i> oxidase (CcO) purified from bovine heart. The inhibition is strongly dependent on concentration of dodecyl-maltoside (DM) in the assay. The plots of K<sub>i</sub> vs [DM] are linear for both estrad...
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doaj-08a92dd933bc4b1e82eec4c67eb14e962020-11-25T03:40:06ZengMDPI AGCells2073-44092020-09-0192211221110.3390/cells9102211Interaction of Cytochrome C Oxidase with Steroid HormonesIlya P. Oleynikov0Natalia V. Azarkina1Tatiana V. Vygodina2Alexander A. Konstantinov3A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Leninskie gory 1, Bld. 40, 119 992 Moscow, RussiaA.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Leninskie gory 1, Bld. 40, 119 992 Moscow, RussiaA.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Leninskie gory 1, Bld. 40, 119 992 Moscow, RussiaA.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Leninskie gory 1, Bld. 40, 119 992 Moscow, RussiaEstradiol, testosterone and other steroid hormones inhibit cytochrome <i>c</i> oxidase (CcO) purified from bovine heart. The inhibition is strongly dependent on concentration of dodecyl-maltoside (DM) in the assay. The plots of K<sub>i</sub> vs [DM] are linear for both estradiol and testosterone which may indicate an 1:1 stoichiometry competition between the hormones and the detergent. Binding of estradiol, but not of testosterone, brings about spectral shift of the oxidized CcO consistent with an effect on heme <i>a</i><sub>3</sub><sup>3+</sup>. We presume that the hormones bind to CcO at the bile acid binding site described by Ferguson-Miller and collaborators. Estradiol is shown to inhibit intraprotein electron transfer between hemes <i>a</i> and <i>a</i><sub>3</sub><sub>.</sub> Notably, neither estradiol nor testosterone suppresses the peroxidase activity of CcO. Such a specific mode of action indicates that inhibition of CcO activity by the hormones is associated with impairing proton transfer via the K-proton channel.https://www.mdpi.com/2073-4409/9/10/2211cytochrome oxidasesteroid hormonesregulation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ilya P. Oleynikov Natalia V. Azarkina Tatiana V. Vygodina Alexander A. Konstantinov |
spellingShingle |
Ilya P. Oleynikov Natalia V. Azarkina Tatiana V. Vygodina Alexander A. Konstantinov Interaction of Cytochrome C Oxidase with Steroid Hormones Cells cytochrome oxidase steroid hormones regulation |
author_facet |
Ilya P. Oleynikov Natalia V. Azarkina Tatiana V. Vygodina Alexander A. Konstantinov |
author_sort |
Ilya P. Oleynikov |
title |
Interaction of Cytochrome C Oxidase with Steroid Hormones |
title_short |
Interaction of Cytochrome C Oxidase with Steroid Hormones |
title_full |
Interaction of Cytochrome C Oxidase with Steroid Hormones |
title_fullStr |
Interaction of Cytochrome C Oxidase with Steroid Hormones |
title_full_unstemmed |
Interaction of Cytochrome C Oxidase with Steroid Hormones |
title_sort |
interaction of cytochrome c oxidase with steroid hormones |
publisher |
MDPI AG |
series |
Cells |
issn |
2073-4409 |
publishDate |
2020-09-01 |
description |
Estradiol, testosterone and other steroid hormones inhibit cytochrome <i>c</i> oxidase (CcO) purified from bovine heart. The inhibition is strongly dependent on concentration of dodecyl-maltoside (DM) in the assay. The plots of K<sub>i</sub> vs [DM] are linear for both estradiol and testosterone which may indicate an 1:1 stoichiometry competition between the hormones and the detergent. Binding of estradiol, but not of testosterone, brings about spectral shift of the oxidized CcO consistent with an effect on heme <i>a</i><sub>3</sub><sup>3+</sup>. We presume that the hormones bind to CcO at the bile acid binding site described by Ferguson-Miller and collaborators. Estradiol is shown to inhibit intraprotein electron transfer between hemes <i>a</i> and <i>a</i><sub>3</sub><sub>.</sub> Notably, neither estradiol nor testosterone suppresses the peroxidase activity of CcO. Such a specific mode of action indicates that inhibition of CcO activity by the hormones is associated with impairing proton transfer via the K-proton channel. |
topic |
cytochrome oxidase steroid hormones regulation |
url |
https://www.mdpi.com/2073-4409/9/10/2211 |
work_keys_str_mv |
AT ilyapoleynikov interactionofcytochromecoxidasewithsteroidhormones AT nataliavazarkina interactionofcytochromecoxidasewithsteroidhormones AT tatianavvygodina interactionofcytochromecoxidasewithsteroidhormones AT alexanderakonstantinov interactionofcytochromecoxidasewithsteroidhormones |
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