Literature DB >> 2831199

Magnetization of the oxidized and reduced three-iron cluster of Desulfovibrio gigas ferredoxin II.

E P Day1, J Peterson, J J Bonvoisin, I Moura, J J Moura.   

Abstract

The saturation magnetizations of the three iron cluster of ferredoxin II of Desulfovibrio gigas in both the oxidized and reduced states have been studied at fixed magnetic fields up to 4.5 tesla over the temperature range from 1.8 to 200 K. The low field (0.3 tesla) susceptibility of oxidized ferredoxin II obeys the Curie law over this entire temperature range. This establishes -2Jox greater than 200 cm-1 as the lower limit for the antiferromagnetic exchange coupling of oxidized ferredoxin II. The saturation magnetizations of reduced ferredoxin II at several fixed fields yield a nested family of curves which can be fit with spin S = 2 and D = -2.7(4) cm-1 (with E/D assigned the value 0.23 as determined by Mössbauer and EPR spectra). The low field susceptibility of reduced ferredoxin II also obeys the Curie law from approximately 4 up to 200 K. This establishes -2Jred greater than 40 cm-1 as the lower limit for the antiferromagnetic coupling of reduced ferredoxin II.

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Year:  1988        PMID: 2831199

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  Investigation of exchange couplings in [Fe3S4]+ clusters by electron spin-lattice relaxation.

Authors:  J Telser; H I Lee; B M Hoffman
Journal:  J Biol Inorg Chem       Date:  2000-06       Impact factor: 3.358

2.  Magnetic circular dichroism study of the selenium-substituted form (Fe3Se4) of bovine heart aconitase.

Authors:  J L Breton; J A Farrar; M C Kennedy; H Beinert; A J Thomson
Journal:  Biochem J       Date:  1995-10-01       Impact factor: 3.857

3.  Measurement of the spin concentration of metalloprotein samples from saturation-magnetization data with particular reference to cytochrome c oxidase.

Authors:  J Peterson; E P Day; L L Pearce; M T Wilson
Journal:  Biochem J       Date:  1995-02-01       Impact factor: 3.857

4.  Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase.

Authors:  K K Surerus; M C Kennedy; H Beinert; E Münck
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

  4 in total

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