Cytochrome c as a Peroxidase: Activation of the Precatalytic Native State by H2O2-Induced Covalent Modifications

2017 ◽  
Vol 139 (44) ◽  
pp. 15701-15709 ◽  
Author(s):  
Victor Yin ◽  
Gary S. Shaw ◽  
Lars Konermann
Keyword(s):  
Cytochrome C ◽  
Native State ◽  
Covalent Modifications ◽  
Peroxidase Activation

Salt as a catalyst in the mitochondria: returning cytochrome c to its native state after it misfolds on the surface of cardiolipin containing membranes

2014 ◽  
Vol 50 (28) ◽  
pp. 3674-3676 ◽  
Author(s):  
Leah A. Pandiscia ◽  
Reinhard Schweitzer-Stenner
Keyword(s):  
Cytochrome C ◽  
Native State ◽  
Unfolded State ◽  
Partially Unfolded

After binding to TOCL/DOPC(20%/80%) liposomes ferricytochrome c remains mostly in its partially unfolded state under folding conditions. The addition of 100 mM NaCl switches it back to the native state.

scholarly journals Cytochrome c folding pathway: Kinetic native-state hydrogen exchange

2002 ◽  
Vol 99 (19) ◽  
pp. 12173-12178 ◽  
Author(s):  
L. Hoang ◽  
S. Bedard ◽  
M. M. G. Krishna ◽  
Y. Lin ◽  
S. W. Englander
Keyword(s):  
Cytochrome C ◽  
Hydrogen Exchange ◽  
Folding Pathway ◽  
Native State

scholarly journals Dramatic shape changes occur as Cytochrome c folds

2020 ◽  
Author(s):  
Serdal Kirmizialtin ◽  
Felicia Pitici ◽  
Alfredo E Cardenas ◽  
Ron Elber ◽  
D. Thirumalai
Keyword(s):  
Cytochrome C ◽  
Experimental Studies ◽  
Quantitative Agreement ◽  
Time Dependent ◽  
Native State ◽  
Time Resolved ◽  
Hydrophobic Collapse ◽  
Folding Mechanism ◽  
Cyt C ◽  
Shape Changes

AbstractExtensive experimental studies on the folding of Cytochrome c (Cyt c) make this small protein an ideal target for atomic detailed simulations for the purposes of quantitatively characterizing the structural transitions and the associated time scales for folding to the native state from an ensemble of unfolded states. We use previously generated atomically detailed folding trajectories by the Stochastic Difference Equation in Length (SDEL) to calculate the time-dependent changes in the Small Angle X-ray scattering (SAXS) profiles. Excellent agreement is obtained between experiments and simulations for the time dependent SAXS spectra, allowing us to identify the structures of the folding intermediates, which shows that Cyt c reaches the native state by a sequential folding mechanism. Using the ensembles of structures along the folding pathways we show that compaction and the sphericity of Cyt c change dramatically from the prolate ellipsoid shape in the unfolded state to the spherical native state. Our data, which provides unprecedented quantitative agreement with all aspects of time-resolved SAXS experiments, shows that hydrophobic collapse and amide group protection coincide on the 100 microseconds time scale, which is in accord with ultrafast Hydrogen/Deuterium exchange studies. Based on these results we propose that compaction of polypeptide chains, accompanied by dramatic shape changes, is a universal characteristic of globular proteins, regardless of the underlying folding mechanism.

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 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.

Existence of DNA in yeast microbodies

1978 ◽  
Vol 36 (2) ◽  
pp. 232-233
Author(s):  
Masako Osumi ◽  
Misuzu Nagano ◽  
Hiroko Kazama
Keyword(s):  
Catalase Activity ◽  
Buoyant Density ◽  
Model System ◽  
Contour Length ◽  
Native State ◽  
Normal Alkane ◽  
Remarkable Increase ◽  
Dna Molecule ◽  
Mitochondrial Dnas

We have found that microbodies appeared profusely together with a remarkable increase in catalase activity in normal alkane-grown cells of hydrocarbon-utilizing Candida yeasts, and that the microbodies multiplied by division in these cells. These features of Candida yeasts seem to provide a useful model system for studies on the biogenesis of the microbody. Subsequently, we have succeeded in isolation of Candida microbodies in an apparently native state, as judged biochemically and morphologically. The presence of DNA in the purified microbody fraction thus obtained was proved by the diphenylamine method. DNA molecule of about 15 urn in contour length was released from an isolated microbody. The physicochemical analyses of the microbody DNA revealed that its buoyant density differed from nuclear and mitochondrial DNAs. All these results lead us to the possibility that there is a novel type of DNA in microbodies.

Electron Microscopic Observation of Biological Specimens in Their Native State by Employing Cryogenic Techniques

1972 ◽  
Vol 30 ◽  
pp. 410-411 ◽  
Author(s):  
Tokio Nei ◽  
Haruo Yotsumoto ◽  
Yoichi Hasegawa ◽  
Yuji Nagasawa
Keyword(s):  
Electron Microscopic Observation ◽  
Surface Structures ◽  
Specimen Preparation ◽  
Native State ◽  
Electron Microscopic ◽  
Biological Specimen ◽  
Specimen Holder ◽  
Cold Stage ◽  
Preparation Techniques ◽  
Scanning Electron

In order to observe biological specimens in their native state, that is, still containing their water content, various methods of specimen preparation have been used, the principal two of which are the chamber method and the freeze method.Using its recently developed cold stage for installation in the pre-evacuation chamber of a scanning electron microscope, we have succeeded in directly observing a biological specimen in its frozen state without the need for such conventional specimen preparation techniques as drying and metallic vacuum evaporation. (Echlin, too, has reported on the observation of surface structures using the same freeze method.)In the experiment referred to herein, a small sliced specimen was place in the specimen holder. After it was rapidly frozen by freon cooled with liquid nitrogen, it was inserted into the cold stage of the specimen chamber.

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