Absolute Configuration of Protochlorophyllide a and Substrate Specificity of NADPH−Protochlorophyllide Oxidoreductase-Reference-Cited by-同舟云学术

Absolute Configuration of Protochlorophyllide a and Substrate Specificity of NADPH−Protochlorophyllide Oxidoreductase

Published:1996-01-01 Issue:11 Volume:118 Page:2606-2611
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Helfrich Michael¹,Schoch Siegrid¹,Schäfer Wolfram¹,Ryberg Margareta¹,Rüdiger Wolfhart¹

Affiliation:

1. Contribution from the Botanisches Institut der Universität München, Menzinger Strasse 67, D-80638 München, Germany, Max-Planck Institut für Biochemie, Am Klopferspitz 18 a, D-82152 Martinsried, Germany, and Department of Plant Physiology, University of Göteborg, Carl Skottsbergs Gata 22, S-41319 Göteborg, Sweden

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja953440c

Reference35 articles.

1. Schulz, R.; Senger, H.Pigment-Protein complexes in plastids. Synthesis and Assembly; Sundqvist, C., Ryberg, M., Eds.; Academic Press: San Diego, 1993; p 179.

2. On the aggregational states of protochlorophyllide and its protein complexes in wheat etioplasts

3. Localization of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies

4. Transitory pigment-protein complexes similar to photosynthesis active centres during protochlorophyll(ide) photoreduction

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