The structure of an electron transfer complex containing a cytochrome c and a peroxidase.
Efficient biological electron transfer may require a fluid association of redox partners. Two noncrystallographic methods (a new molecular docking program and 1H NMR spectroscopy) have been used to study the electron transfer complex formed between the cytochrome c peroxidase (CCP) of Paracoccus denitrificans and cytochromes c. For the natural redox partner, cytochrome c550, the results are consistent with a complex in which the heme of a single cytochrome lies above the exposed electron-transferring heme of the peroxidase. In contrast, two molecules of the nonphysiological but kinetically competent horse cytochrome bind between the two hemes of the peroxidase. These dramatically different patterns are consistent with a redox active surface on the peroxidase that may accommodate more than one cytochrome and allow lateral mobility.
Pettigrew
G W
GW
Department of Preclinical Veterinary studies, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Summerhall Edinburgh EH9 1QH, United Kingdom. graham@lab0.vet.ed.ac.uk
Prazeres
S
S
Costa
C
C
Palma
N
N
Krippahl
L
L
Moura
I
I
Moura
J J
JJ
D000818:Animals; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D004579:Electron Transport; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons
D003574:Cytochrome c Group; D011522:Protons; D010544:Peroxidases