Lys(842) in Neuronal Nitric-oxide Synthase Enables the Autoinhibitory Insert to Antagonize Calmodulin Binding, Increase FMN Shielding, and Suppress Interflavin Electron Transfer

Antzeko izenburuak

• Neutralizing a Surface Charge on the FMN Subdomain Increases the Activity of Neuronal Nitric-oxide Synthase by Enhancing the Oxygen Reactivity of the Enzyme Heme-Nitric Oxide Complex
  nork: Haque, Mohammad Mahfuzul, et al.
  Argitaratua: (2009)
• A Kinetic Model Linking Protein Conformational Motions, Interflavin Electron Transfer, and Electron Flux through a Dual-Flavin Enzyme: Simulating the reductase activity of the endothelial and neuronal NO Synthase flavoprotein domains
  nork: Haque, Mohammad Mahfuzul, et al.
  Argitaratua: (2011)
• Charge Pairing Interactions Control the Conformational Setpoint and Motions of the FMN Domain in Neuronal Nitric Oxide Synthase
  nork: Haque, Mohammad Mahfuzul, et al.
  Argitaratua: (2013)
• A Bridging Interaction Allows Calmodulin to Activate NO Synthase through a Bi-modal Mechanism
  nork: Tejero, Jesús, et al.
  Argitaratua: (2010)
• Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics
  nork: He, Yufan, et al.
  Argitaratua: (2015)