Roland Benz

TL;DR: Detailed analysis indicated that this anionic residue in the phosphate binding site of OprP, despite its negative charge, maintained energetically favorable phosphate binding sites in the central region of the channel and at the same time decreased residence time thus preventing excessively strong binding of phosphate that would oppose phosphate flux through the channel.

TL;DR: It is shown that distinct residues within the vestibule interact with chloroquine and Ia or are responsible for channel structure, while the channel lining amino acids play a less important role, and that T360 has a structural role in the pore organization.

TL;DR: The results suggest that the structure of the porin pore remains essentially unchanged after chemical modification of the pores and that their cation selectivity is caused by an excess of negatively charged groups inside the pore and/or on the surface of the protein.

TL;DR: An extensive immunological comparison of different mitochondrial porins is presented and the possibility of the presence of two different porins in liver mitochondria of Anguilla anguilla is discussed.

TL;DR: Zero-current membrane potential measurements suggested that the second mitochondrial porin is slightly cation-selective, while yeast porin will be slightly anion- selective in the open state but highly cated-selectives in the closed state.