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The low temperature magnetic circular dichroism spectra of iron sulfur proteins part 2 2 iron ferredoxins

, : The low temperature magnetic circular dichroism spectra of iron sulfur proteins part 2 2 iron ferredoxins. Biochimica et Biophysica Acta 493(1): 132-141

Variable temperature magnetic circular dichroism (MCD) spectra of a number of 2-iron ferrodoxins were measured. The spectra of fully oxidized spinach and Spirulina maxima ferredoxin are independent of temperature between room temperature and K, showing that no contribution to the room temperature MCD spectrum arises from the small population of low-lying excited states originating from the exchange coupling. The low temperature MCD spectra of the half-reduced proteins of spinach and S. maxima, ferredoxin and adrenodoxin, are all reasonably intense and temperature dependent. An interpretation of the spectrum of the charge-transfer region is suggested by starting with the assignments previously obtained from rubredoxin.

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