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Showing 1 to 5 of 5 for “"Dinitrosyl iron complexes"”.

  1. Synthetic Analogues of Dinitrosyl Iron Complexes: Reactivity Studies and Improvements towards Therapeutic Applications

    Dinitrosyl iron complexes (DNICs) are organometallic-like compounds formed endogenously as products of degradation of iron-sulfur clusters by NO or its interaction with the cellular chelatable iron pool. Substantial evidence has accrued on the role of DNICs as endogenous transport and storage …

    tamu Repository record for Synthetic Analogues of Dinitrosyl Iron Complexes: Reactivity Studies and Improvements towards Therapeutic Applications (opens in a new tab)

  2. Biogenesis and Redox Transition of Iron-sulfur Clusters in Proteins

    Iron-sulfur proteins comprise one of the most ubiquitous and conserved classes of proteins in biology. The diverse functions of iron-sulfur clusters in proteins range from electron transfer to redox signaling. The assembly of iron-sulfur clusters in cells requires a complex protein system and …

    lsu-thes Repository record for Biogenesis and Redox Transition of Iron-sulfur Clusters in Proteins (opens in a new tab)

  3. Reactions of S-nitrosothiols with biomimetic iron complexes and other transition metals

    … synthases (NOS), NADH, and 02. NOS enzymes have ironporphyrin and biopterin cofactors that catalyze this conversion. S-nitrosothiols form in biology as NO-transport mechanisms, post-translational modifications, or as a cellular protectant against overexposure to NO. Heme and non-heme iron

    mit Repository record for Reactions of S-nitrosothiols with biomimetic iron complexes and other transition metals (opens in a new tab)

  4. Exploring the reactivity of bacterial multicomponent monooxygenases

    … at an active site carboxylate-bridged diiron center. This overview describes structural and biochemical studies of the BMM protein components, presents the proposed mechanisms of 02 activation by BMMs and related carboxylate-bridged diiron proteins, and discuses substrate reactivity of …

    mit Repository record for Exploring the reactivity of bacterial multicomponent monooxygenases (opens in a new tab)