Blum, Ofer and Haiek, Abed and Cwikel, Dory and Dori, Zvi and Meade, Thomas J. and Gray, Harry B. (1998) Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding. Proceedings of the National Academy of Sciences of the United States of America, 95 (12). pp. 6659-6662. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:BLUpnas98
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Reaction of the Schiff-base complex [Co(acetylacetonate-ethylenediimine)(NH3)(2)](+) with metmyoglobin at pH 6.5 yields a partially folded protein containing six Co(III) complexes. Although half of its a-helical secondary structure is retained, absorption and Co spectra indicate that the tertiary structure in both B-F and AGH domains is disrupted in the partially folded protein. In analogy to proton-induced unfolding, it is likely that the loss of tertiary structure is triggered by metal-ion binding to histidines. Cobalt(III)-induced unfolding of myoglobin is unique in its selectivity (other proteins are unaffected) and in allowing the isolation of the partially folded macromolecule (the protein does not refold or aggregate upon removal of free denaturant).
|Additional Information:||Copyright © 1998 by The National Academy of Sciences. Contributed by Harry B. Gray, April 6, 1998. We thank Drs. Bassil Dahiyat and Michel E. Goldberg for discussions. O.B. acknowledges Rothchild and Fulbright postdoctoral fellowships. This work was supported by the National Science Foundation, the Arnold and Mabel Beckman Foundation, and the Redox Pharmaceutical Corporation.|
|Subject Keywords:||protein unfolding, cobalt complexes, SPERM WHALE MYOGLOBIN, CYTOCHROME-C, INTERMEDIATE, APOMYOGLOBIN, PATHWAY, ACID, STABILITY, STATES, HORSE|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||01 Sep 2005|
|Last Modified:||26 Dec 2012 08:40|
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