J. Biochem, 1988, Vol. 103, No. 6 962-968
© 1988 Japanese Biochemical Society
research-article |
The Protein Responsible for Center A/B in Spinach Photosystem I: Isolation with Iron-Sulfur Cluster(s) and Complete Sequence Analysis1
Department of Biology,Osaka University, Toyonaka, Osaka 560
The 9 kDa polypeptide from spinach photosystem I (PS I) complex was isolated with iron-sulfur cluster(s) by an n-butanol extraction procedure under anaerobic conditions. The polypeptide was soluble in a saline solution and contained non-heme irons and inorganic sulfides. The absorption spectrum of this iron-sulfur protein was very similar to those of bacterial-type ferredoxins. The amino acid sequence of the polypeptide was determined by using a combination of gas-phase sequencer and conventional procedures. It was composed of 80 amino acid residues giving a molecular weight of 8, 894, excluding iron and sulfur atoms. The sequence showed the typical distribution of cysteine residues found in bacterial-type ferredoxins and was highly homologous (91% homology) to that deduced from the chloroplast gene, frxA, of liverwort, Marchantia polymorpha. The 9 kDa polypeptide is considered to be the iron-sulfur protein responsible for the electron transfer reaction in PS I from center X to [2Fe-2S] ferredoxin, namely a polypeptide with center(s) A and/or B in PS I complex. It is noteworthy that the 9 kDa polypeptide was rather hydrophilic and a little basic in terms of the primary structure. A three-dimensional structure was simulated on the basis of the tertiary structure of Peptococcus aerogenes [8Fe-8S] ferredoxin, and the portions in the molecule probably involved in contacting membranes or other polypeptides were indicated. The phylogenetic implications of the structure of the present polypeptide as compared with those of several bacterial-type ferredoxins are discussed.
1This work was supported in part by a Grant-in-Aid for Scientific Research on the Priority Area of "Molecular Mechanism of Photoreceptor (No. 62621506)" from the Ministry of Education, Science and Culture of Japan.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  H. Naver, E. Boudreau, and J.-D. Rochaix Functional Studies of Ycf3: Its Role in Assembly of Photosystem I and Interactions with Some of Its Subunits PLANT CELL, December 1, 2001; 13(12): 2731 - 2745. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Naver, M. P. Scott, J. H. Golbeck, C. E. Olsen, and H. V. Scheller The Eight-amino Acid Internal Loop of PSI-C Mediates Association of Low Molecular Mass Iron-Sulfur Proteins with the P700-FX Core in Photosystem I J. Biol. Chem., July 24, 1998; 273(30): 18778 - 18783. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Sun, Q. Xu, V. P. Chitnis, P. Jin, and P. R. Chitnis Topography of the Photosystem I Core Proteins of the Cyanobacterium Synechocystis sp. PCC 6803 J. Biol. Chem., August 29, 1997; 272(35): 21793 - 21802. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Mehari, F. Qiao, M. P. Scott, D. F. Nellis, J. Zhao, D. A. Bryant, and J. H. Golbeck Modified Ligands to F(A) and F(B) in Photosystem I J. Biol. Chem., November 24, 1995; 270(47): 28108 - 28117. [Abstract] [Full Text] [PDF]
|
|