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Structural Characterization of Nitrosomonas europaea Cytochrome c-552 Variants with Marked Differences in Electronic Structure

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33145383" target="_blank" >RIV/61989592:15310/13:33145383 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1002/cbic.201300118" target="_blank" >http://dx.doi.org/10.1002/cbic.201300118</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/cbic.201300118" target="_blank" >10.1002/cbic.201300118</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural Characterization of Nitrosomonas europaea Cytochrome c-552 Variants with Marked Differences in Electronic Structure

  • Original language description

    Nitrosomonas europaea cytochrome c-552 (Ne c-552) variants with the same His/Met axial ligand set but with different EPR spectra have been characterized structurally, to aid understanding of how molecular structure determines heme electronic structure. Visible light absorption, Raman, and resonance Raman spectroscopy of the protein crystals was performed along with structure determination. The structures solved are those of Ne c-552, which displays a "HALS" (or highly anisotropic low-spin) EPR spectrum,and of the deletion mutant Ne N64delta, which has a rhombic EPR spectrum. Two X-ray crystal structures of wild-type Ne c-552 are reported; one is of the protein isolated from N. europaea cells (Ne c-552n, 2.35 ? resolution), and the other is of recombinant protein expressed in Escherichia coli (Ne c-552r, 1.63 ? resolution). Ne N64delta crystallized in two different space groups, and two structures are reported [monoclinic (2.1 ? resolution) and hexagonal (2.3 ? resolution)]. Comparison

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/ED2.1.00%2F03.0058" target="_blank" >ED2.1.00/03.0058: Regional Centre of Advanced Technologies and Materials</a><br>

  • Continuities

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

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    ChemBioChem

  • ISSN

    1439-4227

  • e-ISSN

  • Volume of the periodical

    14

  • Issue of the periodical within the volume

    14

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    11

  • Pages from-to

    "1828?1838"

  • UT code for WoS article

    000325851800018

  • EID of the result in the Scopus database