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Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: (Fe-S) cluster-driven protein rearrangement

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
;  [1];  [2]; ;  [3]; ;  [4]
  1. Univ. of California, Irvine (USA)
  2. Research Institute of Scripps Clinic, La Jolla, CA (USA)
  3. Virginia Polytechnic Institute and State Univ., Blacksburg (USA)
  4. Univ. of Southern California, Los Angeles (USA)
Azotobacter vinelandii ferredoxin I is a small protein that contains one (4Fe-4S) cluster and one (3Fe-4S) cluster. Recently the x-ray crystal structure has been redetermined and the fdxA gene, which encodes the protein, has been cloned and sequenced. Here the authors report the site-directed mutation of Cys-20, which is a ligand of the (4Fe-4S) cluster in the native protein, to alanine and the characterization of the protein product by x-ray crystallographic and spectroscopic methods. The data show that the mutant protein again contains one (4Fe-4S) cluster and one (3Fe-4S) cluster. The new (4Fe-4S) cluster obtains its fourth ligand from Cys-24, a free cysteine in the native structure. The formation of this (4Fe-4S) cluster drives rearrangement of the protein structure.
OSTI ID:
7064361
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 87:2; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English