Abstract
An iron-sulfur protein of approx. 9 kDa has been isolated from spinach chloroplast membranes. Based on iron and sulfide content (∼900 nmol Fe and S2- per mg protein), optical absorbance and low-temperature EPR spectra, it appears that this protein contains 8Fe and 8S2- in two [4Fe4S] clusters. The protein cross-reacts with an antibody raised against a 9 kDa PS I subunit previously identified as the psaC (frxA) gene product. This identity was confirmed by the N-terminal amino acid sequence of the isolated FeS protein. It is concluded that the isolated FeS protein binds PS I centers FeSA and FeSB and that each of these centers contains 4Fe and 4S2-.
Original language | English (US) |
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Pages (from-to) | 293-297 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 229 |
Issue number | 2 |
DOIs | |
State | Published - Mar 14 1988 |
Keywords
- Iron-sulfur center
- P700
- Photosystem I, Ferredoxin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology