Display options
Cite
Rawlings J, Siiman O, Gray HB. Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites. Proc Natl Acad Sci U S A. 1974;71(1):125-7doi: 10.1073/pnas.71.1.125.
Rawlings, J., Siiman, O., & Gray, H. B. (1974). Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites. Proceedings of the National Academy of Sciences of the United States of America, 71(1), 125-7. https://doi.org/10.1073/pnas.71.1.125
Rawlings, J, et al. "Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites." Proceedings of the National Academy of Sciences of the United States of America vol. 71,1 (1974): 125-7. doi: https://doi.org/10.1073/pnas.71.1.125
Rawlings J, Siiman O, Gray HB. Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites. Proc Natl Acad Sci U S A. 1974 Jan;71(1):125-7. doi: 10.1073/pnas.71.1.125. PMID: 16592130; PMCID: PMC387948.
Copy Download .nbib Format: NLM
Share it on

Proc Natl Acad Sci U S A. 1974 Jan;71(1):125-7. doi: 10.1073/pnas.71.1.125.

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

Proceedings of the National Academy of Sciences of the United States of America

J Rawlings, O Siiman, H B Gray

Affiliations

  1. Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, Calif. 91109.

PMID: 16592130 PMCID: PMC387948 DOI: 10.1073/pnas.71.1.125

Abstract

The electronic absorption spectra of oxidized and reduced spinach ferredoxins have been measured between 1200 and 600 nm at low temperature in D(2)O/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 (6)A(1) --> (4)T(1)d-d transition, whereas the 652-nm (15.3 kcm(-1)) feature of reduced ferredoxin could be due either to (5)E --> (3)T(1) in tetrahedral Fe(II)S(4) or an Fe(II) --> Fe(III) intervalence excitation.

References

  1. Biochim Biophys Acta. 1971 Nov 2;253(1):134-52 - PubMed
  2. Biochim Biophys Acta. 1971 Dec 7;253(2):373-84 - PubMed
  3. Nature. 1970 Aug 8;227(5258):574-7 - PubMed
  4. Biochim Biophys Acta. 1971 Nov 2;253(1):110-33 - PubMed
  5. Arch Biochem Biophys. 1967 Oct;122(1):254-6 - PubMed
  6. Arch Biochem Biophys. 1970 Dec;141(2):456-64 - PubMed
  7. Biochim Biophys Acta. 1971 Aug 6;245(1):201-7 - PubMed
  8. J Mol Biol. 1970 Jun 14;50(2):391-406 - PubMed
  9. J Am Chem Soc. 1970 Dec 2;92(24):7195-8 - PubMed
  10. Biochem J. 1971 Apr;122(3):257-65 - PubMed

Publication Types