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      Structural insights for vanadium catecholates and iron‑sulfur clusters obtained from multiple data analysis methods applied to electron spin relaxation data

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      Journal of Inorganic Biochemistry

      Elsevier BV

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          Abstract

          <p class="first" id="P1">Electron paramagnetic resonance (EPR) inversion recovery curves for vanadium catecholates and iron-sulfur clusters were analyzed with three models: the sum of two exponentials, a stretched exponential, and a model-free distribution of exponentials (UPEN). For all data sets studied fits with a stretched exponential were statistically indistinguishable from the sum of two exponentials, and were significantly better than for single exponentials. UPEN provides insights into the structures of the distributions. For a vanadium(IV) tris catecholate the distribution of relaxation rates calculated with UPEN shows the contribution from spectral diffusion at low temperatures. The energy of the local mode for this complex, found from the temperature dependence of the spin lattice relaxation, is consistent with values expected for a metal-ligand vibration. For the [2Fe-2S] <sup>+</sup> cluster in pyruvate formate lyase activating enzyme (PFL-AE) the small stretched exponential β values (0.3) at low temperature and the distributions calculated with UPEN reflect the contribution from a second rapidly relaxing species that could be difficult to detect by continuous wave EPR. The distributions in 1/ <i>T</i> <sub>1</sub> for the [4Fe-4S] <sup>+</sup> clusters in MftC were about a factor of four wider than for the three other systems studied. The very broad distribution of relaxation rates may be due to protein mobility and distributions in electronic energies and local environments for the clusters. UPEN provides insight into several situations that can result in low values of stretch parameter β including contributions from spectral diffusion, overlapping signals from distinguishable clusters, or very wide distributions. </p><p id="P2"> <div class="figure-container so-text-align-c"> <img alt="" class="figure" src="/document_file/7117e82d-755a-4a02-b722-2e4a6bc145f0/PubMedCentral/image/nihms-1539746-f0012.jpg"/> </div> </p>

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          Author and article information

          Journal
          Journal of Inorganic Biochemistry
          Journal of Inorganic Biochemistry
          Elsevier BV
          01620134
          September 2019
          September 2019
          : 110806
          Article
          10.1016/j.jinorgbio.2019.110806
          6859209
          31505439
          © 2019

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