1ds8: Difference between revisions
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'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-NEUTRAL DQAQB STATE WITH THE PROTON TRANSFER INHIBITOR CD2+''' | '''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-NEUTRAL DQAQB STATE WITH THE PROTON TRANSFER INHIBITOR CD2+''' | ||
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[[Category: Okamura, M Y.]] | [[Category: Okamura, M Y.]] | ||
[[Category: Paddock, M L.]] | [[Category: Paddock, M L.]] | ||
[[Category: | [[Category: Bacterial photosynthesis]] | ||
[[Category: | [[Category: Cation binding]] | ||
[[Category: | [[Category: Integral membrane protein]] | ||
[[Category: | [[Category: Metal ion binding]] | ||
[[Category: | [[Category: Proton transfer]] | ||
[[Category: | [[Category: Rhodobacter sphaeroide]] | ||
[[Category: | [[Category: X-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:12:41 2008'' | |||
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Revision as of 14:12, 2 May 2008
PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-NEUTRAL DQAQB STATE WITH THE PROTON TRANSFER INHIBITOR CD2+
OverviewOverview
The reaction center (RC) from Rhodobacter sphaeroides couples light-driven electron transfer to protonation of a bound quinone acceptor molecule, Q(B), within the RC. The binding of Cd(2+) or Zn(2+) has been previously shown to inhibit the rate of reduction and protonation of Q(B). We report here on the metal binding site, determined by x-ray diffraction at 2.5-A resolution, obtained from RC crystals that were soaked in the presence of the metal. The structures were refined to R factors of 23% and 24% for the Cd(2+) and Zn(2+) complexes, respectively. Both metals bind to the same location, coordinating to Asp-H124, His-H126, and His-H128. The rate of electron transfer from Q(A)(-) to Q(B) was measured in the Cd(2+)-soaked crystal and found to be the same as in solution in the presence of Cd(2+). In addition to the changes in the kinetics, a structural effect of Cd(2+) on Glu-H173 was observed. This residue was well resolved in the x-ray structure-i.e., ordered-with Cd(2+) bound to the RC, in contrast to its disordered state in the absence of Cd(2+), which suggests that the mobility of Glu-H173 plays an important role in the rate of reduction of Q(B). The position of the Cd(2+) and Zn(2+) localizes the proton entry into the RC near Asp-H124, His-H126, and His-H128. Based on the location of the metal, likely pathways of proton transfer from the aqueous surface to Q(B) are proposed.
About this StructureAbout this Structure
1DS8 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
ReferenceReference
Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers., Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G, Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1542-7. PMID:10677497 Page seeded by OCA on Fri May 2 14:12:41 2008