All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Electrochemistry and electron paramagnetic resonance spectroscopy of cytochrome c and its heme-disrupted analogs

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F18%3A73582190" target="_blank" >RIV/61989592:15110/18:73582190 - isvavai.cz</a>

  • Alternative codes found

    RIV/00209805:_____/18:00077869

  • Result on the web

    <a href="http://www.sciencedirect.com/science/article/pii/S156753941730364X?via%3Dihub" target="_blank" >http://www.sciencedirect.com/science/article/pii/S156753941730364X?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bioelechem.2017.09.011" target="_blank" >10.1016/j.bioelechem.2017.09.011</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Electrochemistry and electron paramagnetic resonance spectroscopy of cytochrome c and its heme-disrupted analogs

  • Original language description

    Cytochrome c (cyt c) is one of the most studied conjugated proteins due to its electron-transfer properties and ability to regulate the processes involved in homeostasis or apoptosis. Here we report an electrochemical strategy for investigating the electroactivity of cyt c and its analogs with a disrupted heme moiety, i.e. apocytochrome c (acyt c) and porphyrin cytochrome c (pcyt c). The electrochemical data are supplemented with low-temperature and spin-probe electron paramagnetic resonance (EPR) spectroscopy. The main contribution of this report is a complex evaluation of cyt c reduction and oxidation at the level of surface-localized amino acid residues and the heme moiety in a single electrochemical scan. The electrochemical pattern of cyt c is substantially different to both analogs acyt c and pcyt c, which could be applicable in further studies on the redox properties and structural stability of cytochromes and other hemeproteins.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Bioelectrochemistry

  • ISSN

    1567-5394

  • e-ISSN

  • Volume of the periodical

    119

  • Issue of the periodical within the volume

    February

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    6

  • Pages from-to

    136-141

  • UT code for WoS article

    000418312300017

  • EID of the result in the Scopus database

    2-s2.0-85030846989