NMR analysis of the transient complex between membrane photosystem I and soluble cytochrome c(6)
Artikel i vetenskaplig tidskrift, 2005

A structural analysis of the surface areas of cytochrome c(6), responsible for the transient interaction with photosystem I, was performed by NMR transverse relaxation-optimized spectroscopy. The hemeprotein was titrated by adding increasing amounts of the chlorophyllic photosystem, and the NMR spectra of the free and bound protein were analyzed in a comparative way. The NMR signals of cytochrome c(6) residues located at the hydrophobic and electrostatic patches, which both surround the heme cleft, were specifically modified by binding. The backbones of internal residues close to the hydrophobic patch of cytochrome c(6) were also affected, a fact that is ascribed to the conformational changes taking place inside the hemeprotein when interacting with photosystem I. To the best of our knowledge, this is the first structural analysis by NMR spectroscopy of a transient complex between soluble and membrane proteins.

SYNECHOCYSTIS PCC-6803

FLASH ABSORPTION-SPECTROSCOPY

ANABAENA PCC-7119

ESCHERICHIA-COLI

KINETIC-ANALYSIS

PLASTOCYANIN

ANGSTROM

PCC

REDUCTION

RESOLUTION

7119

RELAXATION

Författare

I. Diaz-Moreno

A. Diaz-Quintana

F. P. Molina-Heredia

P. M. Nieto

Örjan Hansson

Göteborgs universitet

M. A De la Rosa

B Göran Karlsson

Chalmers, Kemi- och bioteknik

Journal of Biological Chemistry

Vol. 280 7925-7931

Ämneskategorier

Kemi