Functional modulation of cytochrome C upon specific binding to DNA nanoribbons

A CdS nanocrystal enhanced TiO2 nanotubes (CdS@TiO2 NATs) photoelectrode was prepared via successive ionic layer adsorption and reaction (SILAR) of CdS on the surface of TiO2 NATs. A HS-aptamer owing a specific binding toward cytochrome c was modified onto the CdS@TiO2 NATs, which resulting a decrease in the photoelectrical current intensity. Cytochrome c is therefore quantified based on the decrease in photoelectrical current. High specificity and high sensitivity were obtained with a linear range from 3 pM to 80 nM, and a limit of detection of 2.53 pM.

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Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1323828111 ◽

2014 ◽

Vol 111 (18) ◽

pp. 6648-6653 ◽

Cited By ~ 66

Author(s):

L. J. McClelland ◽

T.-C. Mou ◽

M. E. Jeakins-Cooley ◽

S. R. Sprang ◽

B. E. Bowler

Keyword(s):

Cytochrome C ◽

Peroxidase Activity ◽

Mitochondrial Cytochrome ◽

Mitochondrial Cytochrome C

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Striking Improvement in Peroxidase Activity of Cytochrome c by Modulating Hydrophobicity of Surface-Functionalized Gold Nanoparticles within Cationic Reverse Micelles

Chemistry - A European Journal ◽

10.1002/chem.201202398 ◽

2012 ◽

Vol 18 (47) ◽

pp. 15021-15030 ◽

Cited By ~ 10

Author(s):

Subhabrata Maiti ◽

Krishnendu Das ◽

Sounak Dutta ◽

Prasanta Kumar Das

Keyword(s):

Gold Nanoparticles ◽

Cytochrome C ◽

Peroxidase Activity ◽

Reverse Micelles ◽

Functionalized Gold Nanoparticles

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Efficient mediatorless superoxide sensors using cytochrome c-modified electrodes: surface nano-organization for selectivity and controlled peroxidase activity

Journal of Electroanalytical Chemistry ◽

10.1016/s0022-0728(00)00077-2 ◽

2000 ◽

Vol 484 (2) ◽

pp. 172-181 ◽

Cited By ~ 75

Author(s):

K.Vengatajalabathy Gobi ◽

Fumio Mizutani

Keyword(s):

Cytochrome C ◽

Peroxidase Activity ◽

Modified Electrodes

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The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c

Dalton Transactions ◽

10.1039/c8dt02185f ◽

2018 ◽

Vol 47 (27) ◽

pp. 9128-9135 ◽

Cited By ~ 10

Author(s):

Rinky D. Parakra ◽

Torsten Kleffmann ◽

Guy N. L. Jameson ◽

Elizabeth C. Ledgerwood

Keyword(s):

Cytochrome C ◽

Peroxidase Activity ◽

Human Cytochrome ◽

Human Cytochrome C

Peroxidase activity of cytochrome c is activated and deactivated by methionine 80 oxidation to the sulfoxide and sulfone respectively.

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Cancer-specific binding of a mouse MAb vs. Candida krusei cytochrome c: an antigen recognized by a cancer-associated human MAb HB4C5

Human Antibodies ◽

10.3233/hab-1993-4405 ◽

1993 ◽

Vol 4 (4) ◽

pp. 186-189 ◽

Cited By ~ 3

Author(s):

Kosei Yasumoto ◽

Yuko Setoguchi ◽

Masanori Kamei ◽

Masatoshi Kato ◽

Kikuo Nomoto ◽

...

Keyword(s):

Cytochrome C ◽

Specific Binding ◽

Candida Krusei

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Interaction of Cytochrome C Oxidase with Steroid Hormones

Cells ◽

10.3390/cells9102211 ◽

2020 ◽

Vol 9 (10) ◽

pp. 2211

Author(s):

Ilya P. Oleynikov ◽

Natalia V. Azarkina ◽

Tatiana V. Vygodina ◽

Alexander A. Konstantinov

Keyword(s):

Electron Transfer ◽

Bile Acid ◽

Cytochrome C ◽

Cytochrome C Oxidase ◽

Steroid Hormones ◽

Peroxidase Activity ◽

Spectral Shift ◽

Proton Channel ◽

Dodecyl Maltoside ◽

Bile Acid Binding

Estradiol, testosterone and other steroid hormones inhibit cytochrome c oxidase (CcO) purified from bovine heart. The inhibition is strongly dependent on concentration of dodecyl-maltoside (DM) in the assay. The plots of Ki 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 a33+. 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 a and a3. 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.

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