SOME PROPERTIES OF A BACILLOMYCIN b-CYTOCHROME c COMPLEX

AbstractMany researchers consider a key role in initiation of apoptosis along the mitochondrial pathway to be enhanced by cytochrome c, one of the components of the mitochondrial respiratory chain, which acquires peroxidase activity by forming a complex with phospholipids. Mitochondrial membranes are destroyed affected by the peroxidase reaction catalyzed by this supramolecular nanoparticle, resulting in the release of various proapoptotic factors into the cellular cytoplasm, ultimately leading to the development of an apoptosis pathway. The study of lipoperoxidase activity of the cytochrome c with cardiolipin complex is conducted via activated chemiluminescence. However, prior to this study, no assessment of the potential contribution of free non-heme iron, which can be inserted into the sample, into chemiluminescence of the system of cytochrome c complex with cardiolipin– hydrogen peroxide. It was found during the study process, that chemiluminescence of this system is indeed generated by the activity of the cytochrome c with cardiolipin complex, and the method of activated chemiluminescence is actually suitable for its study. The effect of trolox and dihydroquercetin (taxifolin) as synthetic and natural antioxidants on lipoperoxidase activity of the cytochrome c with cardiolipin complex was as well assessed via application of chemiluminescence activator specific for lipid peroxidation reactions – coumarin-334. A complete inhibition of lipoperoxidase activity for a few minutes with its subsequent full development under the trolox response and its dose-dependent uniform decrease under dihydroquercetin effect was obtained. These findings are promising for the future studies on inhibition of lipoperoxidase activity of this nanoparticle by antioxidants in order to inhibit the inappropriate apoptosis. Peroxidase activity of intact mitochondria in the comparative application of two chemiluminescence activators: coumarin-334 and coumarin-525, was also featured.Significance of the studyThis study proves that the method of activated chemiluminescence is adequate to study the processes occurring in the early stages of apoptosis. Inhibition of lipoperoxidase activity of the cytochrome c with cardiolipin complex by antioxidants was demonstrated. These findings prove that studies on the effect of antioxidants on this supramolecular nanoparticle will eventually lead to discovery of the news means to prevent and treat diseases caused by apoptosis: myocardial infarction, Alzheimer’s disease, Parkinson’s disease, etc.

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A nitric oxide–binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase

Journal of Biological Chemistry ◽

10.1074/jbc.ra119.008788 ◽

2019 ◽

Vol 294 (45) ◽

pp. 16712-16728 ◽

Cited By ~ 2

Author(s):

Mohd Akram ◽

Joachim Reimann ◽

Andreas Dietl ◽

Andreas Menzel ◽

Wouter Versantvoort ◽

...

Keyword(s):

Nitric Oxide ◽

Cytochrome C ◽

Anammox Bacterium ◽

C Complex

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Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex

Biochemistry ◽

10.1021/bi00053a030 ◽

1993 ◽

Vol 32 (2) ◽

pp. 622-627 ◽

Cited By ~ 36

Author(s):

T. E. Meyer ◽

M. Rivera ◽

F. A. Walker ◽

M. R. Mauk ◽

A. G. Mauk ◽

...

Keyword(s):

Electron Transfer ◽

Cytochrome C ◽

Flash Photolysis ◽

Laser Flash Photolysis ◽

Cytochrome B5 ◽

Laser Flash ◽

C Complex

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Location of Cr(III) in the Cr(III)-cytochrome c complex as observed by NMR spectroscopy

FEBS Letters ◽

10.1016/0014-5793(79)80423-8 ◽

1979 ◽

Vol 107 (2) ◽

pp. 427-430 ◽

Cited By ~ 4

Author(s):

Richard L. Petersen ◽

Raj K. Gupta

Keyword(s):

Nmr Spectroscopy ◽

Cytochrome C ◽

C Complex

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A further investigation of the cytochrome b 5–cytochrome c complex

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-003-0479-y ◽

2003 ◽

Vol 8 (7) ◽

pp. 777-786 ◽

Cited By ~ 12

Author(s):

Lucia Banci ◽

Ivano Bertini ◽

Isabella C. Felli ◽

Ludwig Krippahl ◽

Karel Kubicek ◽

...

Keyword(s):

Cytochrome C ◽

Cytochrome B ◽

C Complex

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Novel insights into the taxonomic diversity and molecular mechanisms of bacterial Mn(III) reduction

10.1101/695007 ◽

2019 ◽

Cited By ~ 2

Author(s):

Nadia Szeinbaum ◽

Brook L. Nunn ◽

Amanda R. Cavazos ◽

Sean A. Crowe ◽

Frank J. Stewart ◽

...

Keyword(s):

Cytochrome C ◽

Molecular Mechanisms ◽

Enrichment Culture ◽

Taxonomic Diversity ◽

Extracellular Electron Transfer ◽

Aquatic Environments ◽

Natural Environments ◽

Biological Reduction ◽

Lake Matano ◽

C Complex

SummarySoluble ligand-bound Mn(III) can support anaerobic microbial respiration in diverse aquatic environments. Thus far, Mn(III) reduction has only been associated with certain Gammaproteobacteria. Here, we characterized microbial communities enriched from Mn-replete sediments of Lake Matano, Indonesia. Our results provide the first evidence for biological reduction of soluble Mn(III) outside the Gammaproteobacteria. Metagenome assembly and binning revealed a novel betaproteobacterium, which we designate “Candidatus Dechloromonas occultata.” This organism dominated the enrichment and expressed a porin-cytochrome c complex typically associated with iron-oxidizing Betaproteobacteria and a novel cytochrome c-rich protein cluster (Occ), including an undecaheme putatively involved in extracellular electron transfer. This occ gene cluster was also detected in diverse aquatic bacteria, including uncultivated Betaproteobacteria from the deep subsurface. These observations provide new insight into the taxonomic and functional diversity of microbially-driven Mn(III) reduction in natural environments.Originality-Significance StatementRecent observations suggest that Mn(III)-ligand complexes are geochemically important in diverse aquatic environments. Thus far, microbially-driven Mn(III) reduction has only been associated with Gammaproteobacteria encoding three-component outer-membrane porin-cytochrome c conduits. Here, we demonstrate that Betaproteobacteria dominate in abundance and with respect to protein expression during biologically-mediated Mn(III) reduction in an enrichment culture from an anoxic lacustrine system. Using metaproteomics, we detect for the first time that Betaproteobacteria express a two-component porin-cytochrome c conduit, and an uncharacterized extracellular undecaheme (11-heme) c-type cytochrome. Although this is the first definitive report of an undecaheme within the Betaproteobacteria, we find evidence that they are widespread in uncultivated strains. These results widen the phylogenetic diversity of Mn(III)-reducing bacteria, and provide new insights into potential molecular mechanisms for soluble Mn(III) reduction

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On the use of cytochrome C as an anti-cancer agent

Veterinariya, Zootekhniya i Biotekhnologiya ◽

10.36871/vet.zoo.bio.202105001 ◽

2021 ◽

Vol 1 (5) ◽

pp. 6-13

Author(s):

L. A. Romodin ◽

Keyword(s):

Lipid Peroxidation ◽

Cell Death ◽

Cytochrome C ◽

Effective Means ◽

Target Cells ◽

Programmed Death ◽

Anti Cancer ◽

C Complex ◽

Cancer Agent

As means of cancer therapy, cytochrome C can be used, which can trigger a cascade of apoptotic reactions in the cytosol, as well as its complex with cardiolipin, which triggers lipid peroxidation, which can ultimately lead to cell death by the mechanism of apoptosis or ferroptosis. This article presents the possibility of using cytochrome C and its complex with phospholipids for the treatment of cancer, as well as the main problems associated with this. The main problem is the development of an effective means of delivering a cytotoxic agent to target cells in vivo. If all problems are solved, the use of free cytochrome C should trigger apoptosis of cancer cells, and the cytochrome C complex with cardiolipin or phosphatidic acid should trigger necrosis – like programmed death by the mechanisms of necroptosis, pyroptosis or ferroptosis.

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