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Insights into the relationship between the haem-binding pocket and the redox potential of c 6 cytochromes: four atomic resolution structures of c 6 and c 6 -like proteins from Synechococcus sp. PCC 7002
The structure of cytochrome c 6C from the mesophilic cyanobacterium Synechococcus sp. PCC 7002 has been determined at 1.03 Å resolution. This is the first structural report on the recently discovered cyanobacterial cytochrome c 6 -like proteins found in marine and nitrogen-fixing cyanobacteria. Desp...
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| Published in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2014-11, Vol.70 (11), p.2823-2832 |
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| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
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| Summary: | The structure of cytochrome
c
6C
from the mesophilic cyanobacterium
Synechococcus
sp. PCC 7002 has been determined at 1.03 Å resolution. This is the first structural report on the recently discovered cyanobacterial cytochrome
c
6
-like proteins found in marine and nitrogen-fixing cyanobacteria. Despite high similarity in the overall three-dimensional fold between cytochromes
c
6
and
c
6C
, 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 typical
c
6
cytochromes and results mainly from the substitution of one residue in the haem pocket. Here, high-resolution crystal structures of mutants of both cytochromes
c
6
and
c
6C
are 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 of
c
6
-like cytochromes. |
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| ISSN: | 1399-0047 1399-0047 |
| DOI: | 10.1107/S1399004714013108 |