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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ED2.1.00%2F03.0058" target="_blank" >ED2.1.00/03.0058: Regionální centrum pokročilých technologií a materiálů</a><br>

Návaznosti

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

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

ChemBioChem

ISSN

1439-4227

e-ISSN

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Svazek periodika

14

Číslo periodika v rámci svazku

14

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

"1828?1838"

Kód UT WoS článku

000325851800018

EID výsledku v databázi Scopus

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