Complexity in the redox titration of the dihaem cytochrome c4.
Redox titration of the dihaem, two domain cytochromes c4 from Pseudomonas aeruginosa, Pseudomonas stutzeri and Azotobacter vinelandii showed complex behaviour indicative of the presence of two redox components. In the case of the P. stutzeri cytochrome c4, two spectroscopically distinct components were present during the redox titration. In contrast, cytochrome c-554(548) from a halophilic Paracoccus species is a stable dimer of a monohaem cytochrome which shows close homology to cytochrome c4, but does not show complexity in its redox titration. The presence of chemically distinct haem environments or anti-cooperative interactions between identical haem groups are two possible explanations for the redox complexity of cytochrome c4. The simple redox titration of cytochrome c-554(548) shows that haems situated relatively close together need not interact, but direct cleavage, separation and study of the domains will be necessary to decide whether they do or do not interact in the case of cytochrome c4.
Leitch
F A
FA
Brown
K R
KR
Pettigrew
G W
GW
D000818:Animals; D001395:Azotobacter / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006736:Horses; D008956:Models, Chemical; D010084:Oxidation-Reduction; D010230:Paracoccus / Q000378:metabolism; D011549:Pseudomonas / Q000378:metabolism
D003574:Cytochrome c Group; C034186:cytochrome C4; D006418:Heme