Abstract
A FERREDOXIN-LIKE protein from Azotobacter vinelandii having 6–7 Fe and 6–7 S2− per mol and a molecular weight of 14,000 has been described by Shethna1 and Yoch et al.2. Its biochemical properties3, electron paramagnetic resonance and redox behaviour4,5, and primary sequence6 have also been studied. This work has established that there are two Fe–S centres separated by 0.744 V in reduction potential, one behaving like the [Fe4S4S4Cys] cluster in high-potential iron proteins, the other displaying novel characteristics. The distribution of cysteines in the N-terminal sequence is distinctly non-homologous with clostridial ferredoxins. Extrusion of the Fe–S cores by thiol displacement produces unique species, suggesting the presence of a new chromophore structure7. I report here crystallographic studies of the protein in a tetragonal crystal form which have led to an electron density map at 4.0 Å resolution. This map reveals two Fe–S clusters of clearly different size and shape. It has not been previously shown that this Fe–S protein, or any other, actually contains clusters of differing structure.
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References
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STOUT, C. Structure of the iron–sulphur clusters in Azotobacter ferredoxin at 4.0 Å resolution. Nature 279, 83–84 (1979). https://doi.org/10.1038/279083a0
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DOI: https://doi.org/10.1038/279083a0
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