[Study of the structure of the photosynthetic reaction center of the green thermophilic bacteria Chloroflexus aurantiacus].
Analysis of the Chloroflexus aurantiacus reaction centre (RC) using both protein and recombinant DNA techniques resulted in determination of its polypeptide composition and the primary structures of its two subunits. A model of the polypeptide chains' folding in the membrane is suggested based on: i) homology between L- and M-subunits of Chloroflexus aurantiacus RC and their counterparts in purple bacteria; ii) comparison of their hydropathy plots, and iii) data on the tertiary structures of purple bacteria RCs. The role of a number of functionally important amino acid residues in the RC electron transport activity is discussed. Limited proteolysis of the RC under non-denaturing conditions was used to determine the contribution of the N-terminal regions to its thermal stability.
Kutuzov
M A
MA
Shmukler
B E
BE
Zargarov
A A
AA
Telezhinskaia
I N
IN
Levina
N B
NB
Zolotarev
A S
AS
Abdulaev
N G
NG
D000595:Amino Acid Sequence; D001419:Bacteria / Q000235:genetics*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005798:Genes, Bacterial; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D045322:Photosynthetic Reaction Center Complex Proteins
Izuchenie structury fotosinteticheskogo reaktsionnogo tsentra zelenoĭ termofil'noĭ bakterii Chloroflexus aurantlacus.