Conformational change of cytochrome c (cyt c) caused by interaction with cardiolipin (CL) is an important step during apoptosis, but the underlying mechanism is controversial. To comprehensively clarify the structural transformations of cyt c upon interaction with CL and avoid the unpredictable alias that might come from protein labeling or mutations, the conformation of purified yeast iso-1 cyt c with natural isotopic abundance in different contents of CL was measured by using NMR spectroscopy,...
[NMR paper] Magic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
Magic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
Related Articles Magic angle spinning (31)P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.
Biochim Biophys Acta. 2016 Oct 26;:
Authors: Kooijman EE, Swim LA, Graber ZT, Tyurina YY, Bay?r H, Kagan VE
Abstract
Specific membrane lipid composition is crucial for optimized structural and functional...
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[NMR paper] Insights into the Role of Substrates on the Interaction between Cytochrome b5 and Cytochrome P450 2B4 by NMR.
Insights into the Role of Substrates on the Interaction between Cytochrome b5 and Cytochrome P450 2B4 by NMR.
Related Articles Insights into the Role of Substrates on the Interaction between Cytochrome b5 and Cytochrome P450 2B4 by NMR.
Sci Rep. 2015;5:8392
Authors: Zhang M, Le Clair SV, Huang R, Ahuja S, Im SC, Waskell L, Ramamoorthy A
Abstract
Mammalian cytochrome b5 (cyt b5) is a membrane-bound protein capable of donating an electron to cytochrome P450 (P450) in the P450 catalytic cycle. The interaction between cyt b5 and...
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02-18-2015 06:15 PM
[NMR paper] Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.
Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.
Related Articles Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.
Biochim Biophys Acta. 2014 Aug 25;
Authors: Laage S, Tao Y, McDermott AE
Abstract
The interaction of lipids with subunit c from F1Fo ATP synthase are studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interact and copurify with cardiolipin. Solid state NMR data on oligomeric rings of Fo...
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[NMR paper] Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Sci Rep. 2013 Aug 29;3:2538
Authors: Yamamoto K, Dürr UH, Xu J, Im SC, Waskell L, Ramamoorthy A
Abstract
Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as...
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[NMR paper] Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
J Biomol NMR. 2013 May 25;
Authors: Volkov AN, van Nuland NA
Abstract
Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution....
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[NMR paper] Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle sp
Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study.
Related Articles Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study.
Biochemistry. 1992 Oct 20;31(41):10129-38
Authors: Spooner PJ, Watts A
The influence of cytochrome c binding to cardiolipin bilayers on the motional characteristics of each component has been analyzed by magic-angle spinning (MAS) NMR. Observations were made by NMR of natural abundance 31P, 13C, and 1H nuclei in the lipid as...
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08-21-2010 11:45 PM
[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3880-5
Authors: Spooner PJ, Watts A
31P NMR measurements were conducted to determine the structural and chemical environment of beef heart cardiolipin when bound to cytochrome c. 31P NMR line shapes infer that the majority of lipid remains...
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[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3871-9
Authors: Spooner PJ, Watts A
Deuterium NMR has been used to investigate the structure and dynamic state of cytochrome c complexed with bilayers of cardiolipin. Reductive methylation was employed to prepare lysyl cytochrome c, and deuterium...
NMR Reveals the Conformational Changes of Cytochrome C upon Interaction with Cardiolipin
Linear Mode
