Journal
APPLIED MAGNETIC RESONANCE
Volume 45, Issue 4, Pages 375-387Publisher
SPRINGER WIEN
DOI: 10.1007/s00723-014-0523-9
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Funding
- Russian Foundation for Basic Research [12-04-00346a]
- Presidium of the Russian Academy of Sciences
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Some recent data on the presence of mononuclear dinitrosyl iron complexes (M-DNIC) with persulfide (R-S-S-) ligands with a characteristic electron paramagnetic resonance signal at g(perpendicular to) = 2.35 and g(parallel to|) = 2.02 (g(aver.) = 2.03) in biological systems (e.g., Escherichia coli cells and isolated iron-sulfur proteins) are reviewed. The generation of M-DNIC is controlled by inorganic sulfur (sulfide, S2-) whose binding to thiols gives persulfides. It is suggested that enhanced production of inorganic sulfur is a result of destruction of active centers of iron-sulfur proteins in the presence of NO or NO-containing compounds. Dinitrosyl iron complexes with thiol-containing ligands are the most active participants in this process. Inorganic sulfur may appear in biological systems during the synthesis or resynthesis of active centers of iron-sulfur proteins in response to activation of cysteine desulfurase, the key enzyme in sulfide synthesis from cysteine.
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