ArticleBiophysical journal2004
Interaction of horse heart and thermus thermophilus type c cytochromes with phospholipid vesicles and hydrophobic surfaces.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- The Human CytochromeBiochemistry · 2020Article
- Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Origin of the conformational heterogeneity of cardiolipin-bound cytochrome C.Journal of the American Chemical Society · 2012Article
- Penetration of lysozyme and cytochrome C in lipid bilayer: fluorescent study.The Journal of membrane biology · 2011Article
- Mass-spectrometry based oxidative lipidomics and lipid imaging: applications in traumatic brain injury.Journal of neurochemistry · 2010Review
- Cytochrome c-lipid interactions: new insights from resonance energy transfer.Biophysical journal · 2010Article
- Cytochrome c polymerization by successive domain swapping at the C-terminal helix.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Cytochrome c/cardiolipin relations in mitochondria: a kiss of death.Free radical biology & medicine · 2009Review
- Disruption of the M80-Fe ligation stimulates the translocation of cytochrome c to the cytoplasm and nucleus in nonapoptotic cells.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Interactions of apomyoglobin with membranes: mechanisms and effects on heme uptake.Protein science : a publication of the Protein Society · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding of horse heart cytochrome c (cyt-c) and Thermus thermophilus cytochrome c(552) (cyt-c(552)) to dioleoyl phosphatidylglycerol (DOPG) vesicles was investigated using Fourier transform infrared (FTIR) spectroscopy and turbidity measurements. FTIR spectra revealed that the tertiary structures of both cytochromes became more open when bound to DOPG vesicles, but this was more pronounced for cyt-c. Their secondary structures were unchanged. Turbidity measurements showed important differences in their behavior bound to the negatively charged DOPG vesicles. Both cytochromes caused the liposomes to aggregate and flocculate, but the ways they did so differed. For cyt-c, more than a monolayer was adsorbed onto the liposome surface prior to aggregation due to charge neutralization, whereas cyt c(552) caused aggregation at a protein/lipid ratio well below that required for charge neutralization. Therefore, although cyt-c may cause liposomes to aggregate by electrostatic interaction, cyt-c(552) does not act in this way. FTIR-attenuated total reflection spectroscopy (FTIR-ATR) revealed that cyt-c lost much of its secondary structure when bound to the hydrophobic surface of octadecyltrichlorosilane, whereas cyt-c(552) folds its domains into a beta-structure. This hydrophobic effect may be the key to the difference between the behaviors of the two cytochromes when bound to DOPG vesicles.
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