Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxins
Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxins
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DOI:
10.1111/j.1432-1033.1996.00092.x
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发表时间:
1996-02-15
期刊:
影响因子:
--
通讯作者:
Teixeira, M
中科院分区:
文献类型:
--
作者:
Bentrop, D;Bertini, I;Teixeira, M
The seven-iron ferredoxin from the hyperthermophilic archaeon Desulfurolobus ambivalens has been investigated by one-dimensional and two-dimensional H-1-NMR in its oxidized and dithionite-reduced states. Al iron atoms of both the three-iron and the four-iron cluster are bound to cysteine residues whose hyperfine shifted resonances were characterized. The pattern of these resonances is similar to those from three-iron, four-iron and eight-iron ferredoxins previously described in the literature, but the four-iron cluster has a shift pattern different from that in other seven-iron proteins. A second set of hyperfine-shifted resonances clearly indicates sample heterogeneity, which possibly involves the four-iran cluster. The observation of interresidue NOEs between two different cysteine residues proves the existence of close spatial proximity of the two dusters in D. ambivalens ferredoxin and therefore indicates structural homology to other dicluster ferredoxins. Moreover, this feature is crucial for the sequence-specific assignment of the hyperfine-shifted resonances. The C alpha-C beta-S-Fe dihedral angles of the cysteine residues coordinating the four-iron cluster could be estimated, and the electronic structure of the three-iron cluster is discussed.