Native FMO-reaction center supercomplex in green sulfur bacteria: an electron microscopy study

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F16%3A43890601" target="_blank" >RIV/60076658:12310/16:43890601 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60077344:_____/16:00460503

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs11120-015-0205-y" target="_blank" >http://link.springer.com/article/10.1007%2Fs11120-015-0205-y</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11120-015-0205-y" target="_blank" >10.1007/s11120-015-0205-y</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Native FMO-reaction center supercomplex in green sulfur bacteria: an electron microscopy study

Popis výsledku v původním jazyce

Chlorobaculum tepidum is a representative of green sulfur bacteria, a group of anoxygenic photoautotrophs that employ chlorosomes as the main light-harvesting structures. Chlorosomes are coupled to a ferredoxin-reducing reaction center by means of the Fenna-Matthews-Olson (FMO) protein. While the biochemical properties and physical functioning of all the individual components of this photosynthetic machinery are quite well understood, the native architecture of the photosynthetic supercomplexes is not. Here we report observations of membrane-bound FMO and the analysis of the respective FMO-reaction center complex. We propose the existence of a supercomplex formed by two reaction centers and four FMO trimers based on the single-particle analysis of the complexes attached to native membrane. Moreover, the structure of the photosynthetic unit comprising the chlorosome with the associated pool of RC-FMO supercomplexes is proposed.

Název v anglickém jazyce

Native FMO-reaction center supercomplex in green sulfur bacteria: an electron microscopy study

Popis výsledku anglicky

Chlorobaculum tepidum is a representative of green sulfur bacteria, a group of anoxygenic photoautotrophs that employ chlorosomes as the main light-harvesting structures. Chlorosomes are coupled to a ferredoxin-reducing reaction center by means of the Fenna-Matthews-Olson (FMO) protein. While the biochemical properties and physical functioning of all the individual components of this photosynthetic machinery are quite well understood, the native architecture of the photosynthetic supercomplexes is not. Here we report observations of membrane-bound FMO and the analysis of the respective FMO-reaction center complex. We propose the existence of a supercomplex formed by two reaction centers and four FMO trimers based on the single-particle analysis of the complexes attached to native membrane. Moreover, the structure of the photosynthetic unit comprising the chlorosome with the associated pool of RC-FMO supercomplexes is proposed.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GBP501%2F12%2FG055" target="_blank" >GBP501/12/G055: Centrum fotosyntetického výzkumu</a><br>

Návaznosti

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

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Photosynthesis Research

ISSN

0166-8595

e-ISSN

—

Svazek periodika

128

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

93-102

Kód UT WoS článku

000372322000009

EID výsledku v databázi Scopus

—