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. 1974 Jan;71(1):125–127. doi: 10.1073/pnas.71.1.125

Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites

Jill Rawlings 1, Olavi Siiman 1, Harry B Gray 1,*
PMCID: PMC387948  PMID: 16592130

Abstract

The electronic absorption spectra of oxidized and reduced spinach ferredoxins have been measured between 1200 and 600 nm at low temperature in D2O/ethylene glycol glasses. Relatively weak absorption bands are observed at 720, 820, and 920 nm in oxidized ferredoxin, and at 652, 820, and 920 nm in reduced ferredoxin. The spectral results show that the two Fe(III) centers in oxidized ferredoxin are not equivalent, and that the 820- and 920-nm bands are associated with the nonreducible site. Assignment of the reducible site as tetrahedral Fe(III) is indicated. The 720-nm (13.9 kcm-1) band in oxidized ferredoxin is attributed to an intensity-enhanced 6A1 → 4T1d-d transition, whereas the 652-nm (15.3 kcm-1) feature of reduced ferredoxin could be due either to 5E → 3T1 in tetrahedral Fe(II)S4 or an Fe(II) → Fe(III) intervalence excitation.

Keywords: ligand field spectra, iron-sulfur proteins, iron(III) coordination

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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