Schejter A, Plotkin B
Lady Davis Chair of Biochemistry, Sackler Institute of Molecular Medicine, Sackler Medical School, Tel Aviv University, Israel.
Biochem J. 1988 Oct 1;255(1):353-6.
A comparison of the binding properties of myoglobin and cytochrome c shows that the latter, in the reduced state, has an unusually large affinity for ligands, including thioethers. This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand.
肌红蛋白和细胞色素c结合特性的比较表明,后者在还原状态下对包括硫醚在内的配体具有异常高的亲和力。这解释了亚铁细胞色素c中甲硫氨酸 - 铁键的显著稳定性,这是由于细胞色素c铁将其电子离域到第六个轴向配体轨道的内在能力所致。