NMR analysis of the transient complex between membrane photosystem I and soluble cytochrome c6.

J Biol Chem 2005 Mar 16;280(9):7925-31. Epub 2004 Dec 16.

Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y Consejo de Investigaciones Científicas, Américo Vespucio, Spain.

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.

Download full-text PDF

Source
http://dx.doi.org/10.1074/jbc.M412422200DOI Listing
March 2005
7 Reads

Publication Analysis

Top Keywords

transient complex
8
structural analysis
8
nmr
5
electrostatic patches
4
located hydrophobic
4
hydrophobic electrostatic
4
patches surround
4
surround heme
4
binding backbones
4
modified binding
4
cleft modified
4
heme cleft
4
residues located
4
signals cytochrome
4
spectra free
4
nmr spectra
4
photosystem nmr
4
chlorophyllic photosystem
4
free bound
4
bound protein
4

References

(Supplied by CrossRef)

Curr. Opin. Struct. Biol. 2001

Proc. Natl. Acad. Sci. U. S. A. 1997

J. Am. Chem. Soc. 2002

Annu. Rev. Biophys. Biomol. Struct. 2003

Similar Publications