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Plant and Cell Physiology, 1963, Vol. 4, No. 4 307-322
© 1963

Article

PHOTOSYNTHETIC NITRITE REDUCTASE II. FURTHER PURIFICATION AND BIOCHEMICAL PROPERTIES OF THE ENZYME1

HIROSI HUZISIGE, KIMIYUKI SATOH, KAZUO TANAKA and TAMIKO HAYASIDA

Department of Biology, Faculty of Science Okayama University, Okayama

  1. Further purification of photosynthetic nitrite reductase (PNiR), which catalyzes the transfer of hydrogen (or electron) from the photolytic system to nitrite, is reported in this paper. Chromatography on DEAE- cellulose and Sephadex gel-filtration were effective for the purification of PNiR.
  2. PNiR could be fractionated into two components. It was inferred from the data obtained that one of these components is identical with PPNR, and the other one may probably be a hitherto unreported flavin enzyme containing FMN as prosthetic group.
  3. The properties of these two components of PNiR were described, and the interrelationship between these catalysts and possible intermediary carriers of this electron transfer system was discussed.

1Dedicated to Prof. H. TAMIYA on the occasion of his 60th birthday. This investigation was supported by a Grant in Aid for Fundamental Scientific Research from the Ministry of Education (No. 407130-1961) and a Grant in Aid for Organized Scientific Research from the Ministry of Education (No. 95037-1960), which are gratefully acknowledged here. The authors also wish to acknowledge that the progress of this study was facilitated by a Grant from the KAISEI-KAI. A preliminary report on this work was read before the 25th Annual Meeting of the Botanical Society of Japan (1960, Osaka).

(Received July 1, 1963; )
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