PetH is rate-controlling in the interaction between PetH, a component of the supramolecular complex with photosystem II, and PetF, a light-dependent electron transfer protein.
Cyanobacterial PetH is similar to ferredoxin-NADP(+) oxidoreductase (FNR) of higher plants and comprises 2 components, CpcD-like rod linker and FNR proteins. Here, I show that PetH controls the rate of the interaction with PetF (ferredoxin [Fd1]). Purified recombinant PetH protein, which cut off a CpcD-like rod linker domain, and Fd1 were used in detailed surface plasmon resonance analyses. The interaction between FNR and Fd1 chiefly involved extremely fast binding and dissociation reactions and the FNR affinity for Fd1 was stronger than the Fd1 affinity for FNR. The dissociation constant values were determined as approximately 93.65 microM (FNR) for Fd1 and 1.469 mM (Fd1) for FNR.
Okada
Ken
K
Research Center for Advanced Agrotechnology and Biotechnology, Toyohashi University of Technology, 1-1 Hibarigaoka, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan. okadak@recab.tut.ac.jp
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D000458:Cyanobacteria / Q000235:genetics / Q000378:metabolism*; D042963:Electron Transport Complex II / Q000378:metabolism*; D005287:Ferredoxin-NADP Reductase / Q000235:genetics / Q000378:metabolism*; D005288:Ferredoxins / Q000378:metabolism*; D005420:Flavoproteins / Q000235:genetics / Q000378:metabolism*; D008027:Light; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D005288:Ferredoxins; D005420:Flavoproteins; D005287:Ferredoxin-NADP Reductase; C082502:petH protein, Bacteria; D042963:Electron Transport Complex II