Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7584423 | Food Chemistry | 2018 | 7 Pages |
Abstract
Fe-transferrins/their homologues in ex-vivo mushrooms were identified by ESR spectroscopy at liquid helium temperature, 4â¯K. The ESR fine-structure signals from Grifola frondosa were analyzed by spectral simulation with a full spin-Hamiltonian approach, determining the spin Hamiltonian parameters of the ferric iron species bound in the biological environment: Sâ¯=â¯5/2, gâ¯=â¯(2.045, 2.01, 2.235), |D|â¯=â¯0.28â¯cmâ1, |E/D|â¯=â¯0.05. The zero-field splitting (ZFS) parameters, D- and E-values, are very close to the reported values, |D|â¯=â¯0.25â¯cmâ1 and |E/D|â¯=â¯0.06, for an Fe-transferrin with oxalate anion, and to |D|â¯=â¯0.25â¯cmâ1 and |E/D|â¯=â¯0.04 for one with malonate anion in human sera, suggesting that the Fe3+ species are from Fe-transferrins or their homologues. Quantum chemical calculations of the ZFS tensors for Fe-transferrins were carried out. Fe-transferrins/homologues have been identified for all the mushrooms under study, suggesting that such Fe3+ enzymes are widely distributed in mushrooms.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Shigeaki Nakazawa, Tomomi Kanno, Kenji Sugisaki, Hiromi Kameya, Miki Matsui, Mitsuko Ukai, Kazunobu Sato, Takeji Takui,