Jl. Breton et al., MAGNETIC CIRCULAR-DICHROISM STUDY OF THE SELENIUM-SUBSTITUTED FORM (FE FE3SE4) OF BOVINE HEART ACONITASE, Biochemical journal, 311, 1995, pp. 197-202
The selenium-substituted inactive form of mitochondrial aconitase cont
ains one [3Fe-4Se](1+/0) cluster [Surerus, Kennedy, Beinert and Munck
(1989) Proc. Natl. Acad. Sci, U.S.A. 87, 9846-9850]. This cluster was
studied in both oxidized and reduced states by magnetic CD (MCD) and E
PR spectroscopy. In the MCD spectra, intensity and transition waveleng
th shifts are observed when compared with the spectra of the native [3
Fe-4S](1+0) cluster. These changes are used to differentiate between t
he charge transfer transitions originating from inorganic and cysteiny
l sulphur. Using also the data from the EPR spectra, the spin ground s
tate is assigned as S = 1/2 for the oxidized [3Fe-4Se](1+) cluster and
S = 2 for the reduced [3Fe-4Se](0) cluster.