Amino acid residues responsible for the different pH dependency of cell-specific ferredoxins in the electron transfer reaction with ferredoxin-NADP+ reductase from maize leaves.

Autor:	Kimata-Ariga Y, Tanaka H; Department of Biological Chemistry, College of Agriculture, Graduate School of Sciences and Technology for Innovation, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan., Kuwano S; Department of Biological Chemistry, College of Agriculture, Graduate School of Sciences and Technology for Innovation, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan.
Jazyk:	angličtina
Zdroj:	Journal of biochemistry [J Biochem] 2024 Sep 03; Vol. 176 (3), pp. 237-244.
DOI:	10.1093/jb/mvae043
Abstrakt:	In the chloroplast stroma, dynamic pH changes occur from acidic to alkaline in response to fluctuating light conditions. We investigated the pH dependency of the electron transfer reaction of ferredoxin-NADP+ reductase (FNR) with ferredoxin (Fd) isoproteins, Fd1 and Fd2, which are localized in mesophyll cells and bundle sheath cells, respectively, in the leaves of C4 plant maize. The pH-dependent profile of the electron transfer activity with FNR was quite different between Fd1 and Fd2, which was mainly explained by the opposite pH dependency of the Km value of these Fds for FNR. Replacement of the amino acid residue at position of 65 (D65N) and 78 (H78A) between the two Fds conferred different effect on their pH dependency of the Km value. Double mutations of the two residues between Fd1 and Fd2 (Fd1D65N/H78A and Fd2N65D/A78H) led to the mutual exchange of the pH dependency of the electron transfer activity. This exchange was mainly explained by the changes in the pH-dependent profile of the Km values. Therefore, the differences in Asp/Asn at position 65 and His/Ala at position 78 between Fd1 and Fd2 were shown to be the major determinants for their different pH dependency in the electron transfer reaction with FNR. (© The Author(s) 2024. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.)
Databáze:	MEDLINE
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