Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
The crystal structure at 2.8 Å resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is described and mechanisms for proton pumping are discussed.
Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH
The crystal structure of pH-downregulated NhaA, the main antiporter of Escherichia coli and many enterobacteria is presented and it is proposed that the binding of charged substrates causes an electric imbalance, inducing movements, that permit a rapid alternating-access mechanism.
The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum.
Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis and the first description of the high-resolution structure of an integral membrane protein is presented.
The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping
The crystal structure of the C-family cbb3 oxidase from Pseudomonas stutzeri is reported, which suggests a different redox-driven pumping mechanism from A and B HCOs, and gives insight into why C H COs are catalytically active at low oxygen concentrations.
Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions.
Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.
Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis.
The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 A resolution, and a group of about 10 water molecules is bound near the binding site of the secondary quinone QB.
The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
- M. Marcia, U. Ermler, G. Peng, H. Michel
- BiologyProceedings of the National Academy of Sciences
- 16 June 2009
The structure suggests that FAD is covalently linked to the polypeptide in an unusual way, via a disulfide bridge between the 8-methyl group and Cys-124, which could apply for transferring electrons from sulfide to FAD.
X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis.