Manganese and Cobalt in the Nonheme Metal-binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-inactive Mechanism

Những quyển sách tương tự

• Why copper is preferred over iron for oxygen activation and reduction in heme-copper oxidases
  Bằng: Bhagi-Damodaran, Ambika, et al.
  Được phát hành: (2016)
• Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities
  Bằng: Bhagi-Damodaran, Ambika, et al.
  Được phát hành: (2016)
• Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase
  Bằng: Bhagi-Damodaran, Ambika, et al.
  Được phát hành: (2018)
• Insights into how heme reduction potentials modulate enzymatic activities of a myoglobin-based functional oxidase
  Bằng: Bhagi-Damodaran, Ambika, et al.
  Được phát hành: (2017)
• Systematic Tuning of Heme Redox Potentials and Its Effects on O(2) Reduction Rates in a Designed Oxidase in Myoglobin
  Bằng: Bhagi-Damodaran, Ambika, et al.
  Được phát hành: (2014)