Role of Histidine 78 of leaf ferredoxin in the interaction with ferredoxin-NADP(+) reductase: regulation of pH dependency and negative cooperativity with NADP(H)

In chloroplast stroma, dynamic pH change occurs in response to fluctuating light conditions. We investigated the pH-dependent electron transfer activity between ferredoxin-NADP(+) reductase (FNR) and ferredoxin (Fd) isoproteins from maize leaves. By increasing pH (from 5.5 to 8.5), the electron transfer activity from FNR to photosynthetic-type Fd (Fd1) significantly increased while the activity to nonphotosynthetic type Fd (Fd3) decreased, which was mainly due to their differences in the pH dependency of K-m for Fd. Mutation of His78 of Fd1 to Val, corresponding amino acid residue in Fd3, lost the pH dependency, indicating a regulatory role of the His78 in the interaction with FNR. We previously showed that the interaction between FNR and Fd was weakened by the allosteric binding of NADP(H) on FNR. His78Val Fd1 mutant largely suppressed this negative cooperativity. These results indicate the involvement of Fd1 His78 in pH dependency and negative cooperativity in the interaction with FNR.

Automated summary

In the chloroplast stroma, changes in pH affect the electron transfer activity between ferredoxin-NADP(+) reductase (FNR) and ferredoxin (Fd) isoproteins in maize leaves. Increasing pH leads to increased activity between FNR and photosynthetic-type Fd (Fd1), while activity with nonphotosynthetic type Fd (Fd3) decreases. The His78 amino acid residue in Fd1 plays a regulatory role in its interaction with FNR, as demonstrated by mutation studies.