Evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases: 1H NMR studies of the di-iron derivative of the Fe(III)Zn(II) enzyme from kidney bean.

Lignende værker

• Biochemical Characterization and Subcellular Localization of the Red Kidney Bean Purple Acid Phosphatase.
  af: Cashikar, A. G., et al.
  Udgivet: (1997)
• Modeling the Active Site of the Purple Acid Phosphatase Enzyme with Hetero-Dinuclear Mixed Valence M(II)–Fe(III) [M = Zn, Ni, Co, and Cu] Complexes Supported over a [N6O] Unsymmetrical Ligand
  af: Chandni Pathak, et al.
  Udgivet: (2017-08-01)
• Modeling the Active Site of the Purple Acid Phosphatase Enzyme with Hetero-Dinuclear Mixed Valence M(II)–Fe(III) [M = Zn, Ni, Co, and Cu] Complexes Supported over a [N(6)O] Unsymmetrical Ligand
  af: Pathak, Chandni, et al.
  Udgivet: (2017)
• Genetic diversity and selection of genotypes to enhance Zn and Fe content in common bean
  af: Talukder, Z. I., et al.
  Udgivet: (2010)
• Identification of Tea Plant Purple Acid Phosphatase Genes and Their Expression Responses to Excess Iron
  af: Chaoyan Yin, et al.
  Udgivet: (2019-04-01)