Open AccessCluster characterization in iron-sulfur proteins by magnetic circular dichroism.
Author(s) -
Philip J. Stephens,
Andrew J. Thomson,
Timothy A. Keiderling,
J. Rawlings,
Krishna Rao,
D.O. Hall
Publication year - 1978
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.11.5273
Subject(s) - ferredoxin , chromatium , sulfur , magnetic circular dichroism , iron–sulfur cluster , circular dichroism , chemistry , crystallography , cluster (spacecraft) , biochemistry , spectral line , enzyme , organic chemistry , computer science , programming language , astronomy , physics
We report magnetic circular dichroism (MCD) spectra of 4-Fe iron-sulfur clusters in the iron-sulfur proteins Chromatium high-potential iron protein (HIPIP), Bacillus stearothermophilus ferredoxin and Clostridium pasteurianum ferredoxin. The MCD is found to vary significantly with cluster oxidation state but is relatively insensitive to the nature of the protein. The spectra obtained are compared with the corresponding spectra of iron-sulfur proteins containing 2-Fe clusters. It is concluded that MCD is useful for the characterization of iron-sulfur cluster type and oxidation state in iron-sulfur proteins and is superior for this purpose to absorption and natural circular dichroism spectroscopy.
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