Peroxidase Activity of Cytochrome c Generated by Phenylboronic Acid Modification

1995 ◽  
Vol 24 (7) ◽  
pp. 529-530 ◽  
Author(s):  
Itaru Hamachi ◽  
Onari Kimura ◽  
Hiroshi Takeshita ◽  
Seiji Shinkai
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Phenylboronic Acid ◽  
Acid Modification

scholarly journals Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity

2014 ◽  
Vol 111 (18) ◽  
pp. 6648-6653 ◽  
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

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

2018 ◽  
Vol 47 (27) ◽  
pp. 9128-9135 ◽  
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.

Functional modulation of cytochrome C upon specific binding to DNA nanoribbons

2019 ◽  
Vol 55 (93) ◽  
pp. 14074-14077
Author(s):  
Xiangyuan Ouyang ◽  
Si-Yao Wang ◽  
Ting Liu ◽  
Yong-An Ren ◽  
Mei-Fang Wang ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Specific Binding ◽  
Redox Activity ◽  
Functional Modulation

We discovered that the redox activity of cytochrome C can be enhanced and its peroxidase activity can be decreased by DNA nanoribbons.

scholarly journals Interaction of Cytochrome C Oxidase with Steroid Hormones

Cells ◽  
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.

The Met80Ala point mutation enhances the peroxidase activity of immobilized cytochrome c

2012 ◽  
Vol 2 (11) ◽  
pp. 2206 ◽  
Author(s):  
Antonio Ranieri ◽  
Fabrizio Bernini ◽  
Carlo Augusto Bortolotti ◽  
Elena Castellini
Keyword(s):  
Cytochrome C ◽  
Point Mutation ◽  
Peroxidase Activity

Heme-octapeptide of cytochrome-c with peroxidase activity coupled to antibody: An alternative method

1975 ◽  
Vol 12 (10) ◽  
pp. 847-848 ◽  
Author(s):  
Heinz A. Gerber ◽  
Thomas Schaffner ◽  
Max W. Hess
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Alternative Method

scholarly journals Antioxidant activity evaluation by physiologically relevant assays based on haemoglobin peroxidase activity and cytochrome c-induced oxidation of liposomes

2015 ◽  
Vol 30 (11) ◽  
pp. 1315-1319 ◽  
Author(s):  
Augustin C. Mot ◽  
Cristina Bischin ◽  
Bianca Muresan ◽  
Marcel Parvu ◽  
Grigore Damian ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Cytochrome C ◽  
Peroxidase Activity ◽  
Activity Evaluation
Sign in / Sign up

Export Citation Format

Share Document