Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 75:662-664 (1984)
© 1984 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fuesler, T. P.
Right arrow Articles by Castelfranco, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fuesler, T. P.
Right arrow Articles by Castelfranco, P. A.
Agricola
Right arrow Articles by Fuesler, T. P.
Right arrow Articles by Castelfranco, P. A.
Articles

Localization of Mg-Chelatase and Mg-Protoporphyrin IX Monomethyl Ester (Oxidative) Cyclase Activities within Isolated, Developing Cucumber Chloroplasts 1

Thomas P. Fuesler, Yum-Shing Wong and Paul A. Castelfranco

Department of Botany, University of California, Davis, California 95616

Magnesium chelatase and magnesium protoporphyrin IX monomethyl ester (oxidative) cyclase activities were both sensitive to inhibition by p-chloromercuribenzoate in intact, developing cucumber (Cucumis sativus L. var Beit Alpha) chloroplasts. Magnesium chelatase was also sensitive to the membrane-impermeable mercurial p-chloromercuribenzene sulfonate (PCMBS), while cyclase activity was only slightly sensitive. When the plastids were pretreated with PCMBS, triosephosphate dehydrogenase activity was inhibited very slightly, indicating that PCMBS does not readily penetrate through the chloroplast envelope. These results suggest that magnesium chelatase is located in the chloroplast envelope, while the cyclase is located deeper within the chloroplast.


1 Supported by National Science Foundation Grant PCM 81-08538.




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
A. Ikegami, N. Yoshimura, K. Motohashi, S. Takahashi, P. G. N. Romano, T. Hisabori, K.-i. Takamiya, and T. Masuda
The CHLI1 Subunit of Arabidopsis thaliana Magnesium Chelatase Is a Target Protein of the Chloroplast Thioredoxin
J. Biol. Chem., July 6, 2007; 282(27): 19282 - 19291.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. D. Willows and S. I. Beale
Heterologous Expression of the Rhodobacter capsulatus BchI, -D, and -H Genes That Encode Magnesium Chelatase Subunits and Characterization of the Reconstituted Enzyme
J. Biol. Chem., December 18, 1998; 273(51): 34206 - 34213.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1984 by the American Society of Plant Biologists