Abstract
RECENTLY, Gillard, McKenzie, Mason, Mayhew, Peel and Stangroom1 presented optical rotatory dispersion data on non-haem iron proteins from several sources. They found that whereas the bacterial ferredoxins from Clostridium acidi-urici, C. pasteurianum and Peptostreptococcus elsdenii and the rubredoxin from P. elsdenii have very similar optical rotatory dispersion spectra in both the oxidized and reduced forms, these spectra differ qualitatively from that obtained with oxidized plant (parsley and spinach) ferredoxin. No data were presented on reduced plant ferredoxin, and indeed it has been reported2 that reduced plant ferredoxin has no optical activity in the visible region of the spectrum. Gillard et al. consequently suggested “that the bonding of iron in plant ferredoxin is entirely different from that in bacterial ferredoxin and rubredoxin”.
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References
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PALMER, G., BRINTZINGER, H. Nature of the Non-haem Iron in Ferredoxin and Rubredoxin. Nature 211, 189–190 (1966). https://doi.org/10.1038/211189a0
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DOI: https://doi.org/10.1038/211189a0
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