Heme–Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case
Molecules, 2022 Heme proteins are known to perform a plethora of biologically important functions. This article reviews work that has been conducted on various class I cytochrome c proteins over a period of nearly 50 years.
Reinhard Schweitzer-Stenner
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Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging
Frontiers in Cell and Developmental Biology, 2022 The normal functioning of sperm cells requires cytochrome c in the redox balanced forms: reduced and oxidized. The oxidized form of cytochrome c is localized in the mitochondrial intermembrane space and is a part of the electron transport chain.
Halina Abramczyk +4 more
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NMR Study on the Mechanism of Cytochrome c Methionine Oxidation
Chinese Journal of Magnetic Resonance, 2023 Mitochondria generate reactive oxygen species (ROS) during respiration. Low levels of ROS are conducive to signal transduction, whereas excessive accumulation of ROS can lead to protein oxidative modification.
ZHAO Beibei +5 more
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Phosphorylation disrupts long-distance electron transport in cytochrome c [PDF]
, 2022 It has been recently shown that electron transfer between mitochondrial cytochrome c and the cytochrome c(1) subunit of the cytochrome bc(1) can proceed at long-distance through the aqueous solution.
Díaz Moreno, Irene +25 more
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Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c‐type cytochromes [PDF]
Molecular Microbiology, 2006 SummaryIn all organisms, haem is post‐translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c‐type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem–apocytochrome ligation per se.
Serdar, Turkarslan +2 more
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Frontiers in Pharmacology, 2021 The enhanced inhibitory effect of paclitaxel (PTX) combined with hypericin (HY) on B16-F10 cells may be realized through the ROS-related cytochrome c release pathway.
Liyun Sun +3 more
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Heme-a, the heme prosthetic group of cytochrome c oxidase, is increased in Alzheimer's disease [PDF]
Neuroscience Letters, 2009 Heme-a, is the heme prosthetic group of cytochrome c oxidase (COX), the terminal complex of the mitochondrial electron transport chain. We measured heme-a levels in postmortem brain tissue from nine patients diagnosed with dementia: Alzheimer's disease (AD) was the primary diagnosis in five, AD/diffuse Lewy body disease (DLBD) was diagnosed in two ...
Barney E, Dwyer +6 more
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Unfolded States of Heme Proteins [PDF]
, 2010 Cytochromes adopt discrete structures when the heme cofactor is present. Since the heme provides crucial contacts in the native protein, this hydrophobic prosthetic group plays an important role in the folding mechanism and introduces interesting ...
Pribisko Yen, Melanie Anne
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Characterization of the cytochrome [beta] gene in plant pathogenic, basidiomycetes and consequences for QoI resistance [PDF]
, 2005 Strobilurins are one of the most important classes of agricultural fungicides, which are also known as Qo inhibitors (QoIs) because they inhibit mitochondrial respiration by binding to the Qo (‘Quinone outside’) site of the cytochrome b.
Grasso, Valeria
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Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase [PDF]
, 2007 All 13 lipids, including two cardiolipins, one phosphatidylcholine, three phosphatidylethanolamines, four phosphatidylglycerols and three triglycerides, were identified in a crystalline bovine heart cytochrome c oxidase (CcO) preparation.
Terada, Hirohito +13 more
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