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J. Biochem, 2003, Vol. 134, No. 2 239-244
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Crystal Structure of Chloroplastic Ascorbate Peroxidase from Tobacco Plants and Structural Insights into its Instability

Kei Wada1, Toshiji Tada*,1, Yoshihiro Nakamura1, Takahiro Ishikawa2, Yukinori Yabuta3, Kazuya Yoshimura3, Shigeru Shigeoka3 and Keiichiro Nishimura1

1 Research Institute for Advanced Science and Technology, Osaka Prefecture University, Gakuen-cho 1-2, Sakai, Osaka 599-8570; 2 Faculty of Life and Environmental Science, Shimane University, Matsue, Shimane 690-8504; and 3 Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nakamachi, Nara 631-8505

Ascorbate peroxidase (APX) is a heme-containing protein that plays a central role in scavenging H2O2 in higher plants. The structure of stromal APX (sAPX) was determined at 1.6 Å to an R-factor of 19.1% and an R-free-factor of 22.3%. The electrostatic potential of the {gamma}-channel that connects the molecular surface of sAPX to the {gamma}-edge of heme was more positive than that of cytosolic APX (cAPX) from pea, so sAPX might bind more easily with ascorbate than cAPX. The overall structure of sAPX was similar to those of cAPX from pea and cytochrome c peroxidase (CCP) from yeast, with a substantial difference in a loop structure located in the vicinity of the heme. The side chain of Arg169 in sAPX corresponding to His169 in cAPX and His181 in CCP extended in the opposite direction from the heme, forming two hydrogen bonds with carbonyl groups in the loop structure. The rapid inactivation of sAPX might be due to the characteristic conformation of Arg169 owing to the loop structure of sAPX.

* To whom correspondence should be addressed. Tel: +81-72-254-9820, Fax: +81-72-252-6776, E-mail: tada{at}riast.osakafu-u.ac.jp


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