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Five Nitrogen Oxidation States from Nitro to Amine: Stabilization and Reactivity of a Metastable Arylhydroxylamine Complex.

Author(s): Zsombor-Pindera J; Effaty F; Escomel L; Patrick B; Kennepohl P; Ottenwaelder X;

Redox noninnocent ligands enhance the reactivity of the metal they complex, a strategy used by metalloenzymes and in catalysis. Herein, we report a series of copper complexes with the same ligand framework, but with a pendant nitrogen group that spans five ...

Article GUID: 33124796

Scavenging with TEMPO* to identify peptide- and protein-based radicals by mass spectrometry: advantages of spin scavenging over spin trapping.

Author(s): Wright PJ, English AM

J Am Chem Soc. 2003 Jul 16;125(28):8655-65 Authors: Wright PJ, English AM

Article GUID: 12848573

Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein.

Author(s): Romeo AA, Capobianco JA, English AM

J Am Chem Soc. 2003 Nov 26;125(47):14370-8 Authors: Romeo AA, Capobianco JA, English AM

Article GUID: 14624585

Lipid binding to the carotenoid binding site in photosynthetic reaction centers.

Author(s): Deshmukh SS, Tang K, Kálmán L

J Am Chem Soc. 2011 Oct 12;133(40):16309-16 Authors: Deshmukh SS, Tang K, Kálmán L

Article GUID: 21894992

LC-MS/MS Proteoform Profiling Exposes Cytochrome c Peroxidase Self-Oxidation in Mitochondria and Functionally Important Hole Hopping from Its Heme

Author(s): Kathiresan M; English AM;

LC-MS/MS profiling reveals that the proteoforms of cytochrome c peroxidase (Ccp1) isolated from respiring yeast mitochondria are oxidized at numerous Met, Trp, and Tyr residues. In vitro oxidation of recombinant Ccp1 by H2O2 in the absence of its reducing s...

Article GUID: 30145880


Title:Lipid binding to the carotenoid binding site in photosynthetic reaction centers.
Authors:Deshmukh SSTang KKálmán L
Link:https://www.ncbi.nlm.nih.gov/pubmed/21894992?dopt=Abstract
Category:J Am Chem Soc
PMID:21894992
Dept Affiliation: PHYSICS
1 Department of Physics, Concordia University, Montreal, Quebec H4B 1R6, Canada.

Description:

Lipid binding to the carotenoid binding site in photosynthetic reaction centers.

J Am Chem Soc. 2011 Oct 12;133(40):16309-16

Authors: Deshmukh SS, Tang K, Kálmán L

Abstract

Lipid binding to the carotenoid binding site near the inactive bacteriochlorophyll monomer was probed in the reaction centers of carotenoid-less mutant, R-26 from Rhodobacter sphaeroides. Recently, a marked light-induced change of the local dielectric constant in the vicinity of the inactive bacteriochlorophyll monomer was reported in wild type that was attributed to structural changes that ultimately lengthened the lifetime of the charge-separated state by 3 orders of magnitude (Deshmukh, S. S.; Williams, J. C.; Allen, J. P.; Kalman, L. Biochemistry 2011, 50, 340). Here in the R-26 reaction centers, the combination of light-induced structural changes and lipid binding resulted in a 5 orders of magnitude increase in the lifetime of the charge-separated state involving the oxidized dimer and the reduced primary quinone in proteoliposomes. Only saturated phospholipids with fatty acid chains of 12 and 14 carbon atoms long were bound successfully at 8 °C by cooling the reaction center protein slowly from room temperature. In addition to reporting a dramatic increase of the lifetime of the charge-separated state at physiologically relevant temperatures, this study reveals a novel lipid binding site in photosynthetic reaction center. These results shed light on a new potential application of the reaction center in energy storage as a light-driven biocapacitor since the charges separated by ~30 Å in a low-dielectric medium can be prevented from recombination for hours.

PMID: 21894992 [PubMed - indexed for MEDLINE]