Insights into the relationship between the haem-binding pocket and the redox potential ofc6cytochromes: four atomic resolution structures ofc6andc6-like proteins fromSynechococcussp. PCC 7002
The structure of cytochromec6Cfrom the mesophilic cyanobacteriumSynechococcussp. PCC 7002 has been determined at 1.03 Å resolution. This is the first structural report on the recently discovered cyanobacterial cytochromec6-like proteins found in marine and nitrogen-fixing cyanobacteria. Despite high similarity in the overall three-dimensional fold between cytochromesc6andc6C, the latter shows saliently different electrostatic properties in terms of surface charge distribution and dipole moments. Its midpoint redox potential is less than half of the value for typicalc6cytochromes and results mainly from the substitution of one residue in the haem pocket. Here, high-resolution crystal structures of mutants of both cytochromesc6andc6Care presented, and the impact of the mutation of specific residues in the haem-binding pocket on the redox potential is discussed. These findings contribute to the elucidation of the structure–function relationship ofc6-like cytochromes.