Universal Stress Protein Regulates Electron Transferand Superoxide Generation Activities of the Cytochrome bc1 Complex from Rhodobacter sphaeroides
Universal Stress Protein Regulates Electron Transferand Superoxide Generation Activities of the Cytochrome bc1 Complex from Rhodobacter sphaeroides
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00658/20151208/images/medium/bi-2015-006587_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00658
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12-10-2015 01:09 AM
Bacteriopheophytin a in the active branch of the reaction center of rhodobacter sphaeroides is not disturbed by the protein matrix as shown by 13C photo-CIDNP MAS NMR
From The DNP-NMR Blog:
Bacteriopheophytin a in the active branch of the reaction center of rhodobacter sphaeroides is not disturbed by the protein matrix as shown by 13C photo-CIDNP MAS NMR
Sai Sankar Gupta, K.B., et al., Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter sphaeroides Is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR. The Journal of Physical Chemistry B, 2013. 117(12): p. 3287-3297.
http://www.ncbi.nlm.nih.gov/pubmed/23452037
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We report NMR data indicating that the Rieske protein from the cytochrome bc complex of Thermus thermophilus (TtRp) undergoes modest redox-state-dependent and ligand-dependent conformational changes. To test...
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[NMR paper] Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter Sphaeroides is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR.
Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter Sphaeroides is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR.
Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter Sphaeroides is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR.
J Phys Chem B. 2013 Mar 1;
Authors: Sai Sankar Gupta KB, Alia A, Buda F, de Groot HJ, Matysik J
Abstract
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Proteins with multiple binding sites exhibit a complex behavior that depends on the intrinsic affinities for each site and the energetic communication between the sites. The contributions from intrinsic affinity and cooperativity are difficult to...
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[NMR paper] Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynt
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[NMR paper] Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynt
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Binding and Energetics of Electron Transfer betweenan Artificial Four-Helix Mn-Protein and Reaction Centers from Rhodobacter sphaeroides
Linear Mode
