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NMR analysis of the transient complex between membrane photosystem I and soluble cytochrome c(6)

I. Diaz-Moreno ; A. Diaz-Quintana ; F. P. Molina-Heredia ; P. M. Nieto ; Örjan Hansson ; M. A De la Rosa ; B Göran Karlsson (Institutionen för kemi- och bioteknik)
Journal of Biological Chemistry Vol. 280 (2005), 9, p. 7925-7931.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: FLASH ABSORPTION-SPECTROSCOPY, SYNECHOCYSTIS PCC-6803, ANGSTROM, RESOLUTION, ANABAENA PCC-7119, ESCHERICHIA-COLI, KINETIC-ANALYSIS, PCC, 7119, PLASTOCYANIN, RELAXATION, REDUCTION



Denna post skapades 2007-10-24. Senast ändrad 2009-11-13.
CPL Pubid: 57067

 

Institutioner (Chalmers)

Institutionen för kemi (2001-2011)
Institutionen för kemi- och bioteknik (2005-2014)

Ämnesområden

Kemi

Chalmers infrastruktur