scholarly journals Lysine carbonylation is a previously unrecognized contributor to peroxidase activation of cytochrome c by chloramine-T

2019 ◽  
Vol 10 (8) ◽  
pp. 2349-2359 ◽  
Author(s):  
Victor Yin ◽  
Safee H. Mian ◽  
Lars Konermann
Keyword(s):  
Cytochrome C ◽  
Ion Mobility ◽  
Peroxidase Activity ◽  
Tandem Ms ◽  
Chloramine T ◽  
Peroxidase Activation

Ion mobility-assisted tandem MS uncovers hitherto overlooked modifications that are critical for the peroxidase activity of chloramine T-modified cytochrome c.

scholarly journals Activation of Cytochrome C Peroxidase Function Through Coordinated Foldon Loop Dynamics upon Interaction with Anionic Lipids

2021 ◽  
Author(s):  
Mingyue Li ◽  
Wanyang Sun ◽  
Vladimir A. Tyurin ◽  
Maria DeLucia ◽  
Jinwoo Ahn ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Magic Angle ◽  
List Type ◽  
Mitochondrial Apoptosis ◽  
Chemical Denaturation ◽  
Cyt C ◽  
Anionic Lipids ◽  
Lipid Peroxidase ◽  
Peroxidase Activation

ABSTRACTCardiolipin (CL) is a mitochondrial anionic lipid that plays important roles in the regulation and signaling of mitochondrial apoptosis. CL peroxidation catalyzed by the assembly of CL-cytochrome c (cyt c) complexes at the inner mitochondrial membrane is a critical checkpoint. The structural changes in the protein, associated with peroxidase activation by CL and different anionic lipids, are not known at a molecular level. To better understand these peripheral protein-lipid interactions, we compare how phosphatidylglycerol (PG) and CL lipids trigger cyt c peroxidase activation, and correlate functional differences to structural and motional changes in membrane-associated cyt c. Structural and motional studies of the bound protein are enabled by magic angle spinning solid state NMR spectroscopy, while lipid peroxidase activity is assayed by mass spectrometry. PG binding results in a surface-bound state that preserves a nativelike fold, which nonetheless allows for significant peroxidase activity, though at a lower level than binding its native substrate CL. Lipid-specific differences in peroxidase activation are found to correlate to corresponding differences in lipid-induced protein mobility, affecting specific protein segments. The dynamics of omega loops C and D are upregulated by CL binding, in a way that is remarkably controlled by the protein:lipid stoichiometry. In contrast to complete chemical denaturation, membrane-induced protein destabilization reflects a destabilization of select cyt c foldons, while the energetically most stable helices are preserved. Our studies illuminate the interplay of protein and lipid dynamics in the creation of lipid peroxidase-active proteolipid complexes implicated in early stages of mitochondrial apoptosis.GRAPHICAL ABSTRACTHIGHLIGHTSA mitochondrial protein-lipid complex regulates lipid peroxidation in apoptosis.Peroxidase-active lipid-cytochrome c complexes are reconstituted in vitro.Phosphatidylglycerol lipids are less effective activators than cardiolipin.Activity correlates to localized dynamics, distinct from chemical denaturation.A dynamic interplay of cytochrome c foldons and anionic lipids regulate activity.

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
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