Insights into the relationship between the haem-binding pocket and the redox potential of c₆ cytochromes: four atomic resolution structures of c₆ and c₆-like proteins from Synechococcus sp. PCC 7002

Atomic resolution structures of cytochromes c₆ and c_6C from Synechococcus sp. PCC 7002 as well as their haem-pocket point mutants are presented. The biophysical and structural properties of these proteins have been characterized with particular focus on the relationship between the structure of the haem-binding pocket and the redox potential.

Structure of a proteolytically resistant analogue of (NLys)⁵SFTI-1 in complex with trypsin: evidence for the direct participation of the Ser214 carbonyl group in serine protease-mediated proteolysis

The structure of a peptide–peptoid analogue inhibitor was determined by X-ray crystallography. It is the first structure to reveal the structural basis of the complete proteolytic resistance towards serine proteases by inhibitors containing a peptoid residue at the P1 position.