The 110-kDa reaction center protein of photosystem-I, P700-chlorophyll A-protein-1, is an iron-sulfur protein

Høj, Peter Bordier and Møller, Birger Lindberg (1986) The 110-kDa reaction center protein of photosystem-I, P700-chlorophyll A-protein-1, is an iron-sulfur protein. Journal of Biological Chemistry, 261 30: 14292-14300.

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Author Høj, Peter Bordier
Møller, Birger Lindberg
Title The 110-kDa reaction center protein of photosystem-I, P700-chlorophyll A-protein-1, is an iron-sulfur protein
Formatted title
The 110-kDa reaction center protein of photosystem-I, P700-chlorophyll α-protein-1, is an iron-sulfur protein

Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1986-10-25
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 261
Issue 30
Start page 14292
End page 14300
Total pages 9
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Abstract Germination and growth of barley (Hordeum vulgare L.) in the presence of 59Fe2+ or 35SO4(2-) allows heavy incorporation of both isotopes into the thylakoid membranes and into isolated photosystem I particles. Analysis of 59Fe-labeled preparations by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under mild conditions demonstrates that a minimum of four iron atoms/P700 is carried on P700-chlorophyll a-protein 1. When isolated from 35S-labeled preparations, P700-chlorophyll a-protein 1 binds zero valence 35S, which is converted into acid-labile [35S]sulfide by dithiothreitol reduction. Isolated photosystem I particles contain 14 acid-labile sulfide atoms and 10 iron atoms for each molecule of P700 and are composed of polypeptides of 110, 18, 15, 10, and 8 kDa of which the 10-kDa component is loosely bound. Under the electrophoretic conditions used, none of the low molecular weight polypeptides could be shown to be specifically associated with iron or acid-labile sulfide. Carboxymethylation of cysteine residues shows a high cysteine content in the 8-kDa polypeptide and an intermediate content in the 110- and 18-kDa polypeptides, whereas the 15-kDa polypeptide is devoid of sulfur amino acids. The experiments with the 59Fe-labeled thylakoids reveal other labeled polypeptides not associated with photosystem I, namely cytochrome f and possibly cytochromes b6 and b559.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Office of the Vice-Chancellor
 
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