Sulfur denitrosylation by an engineered Trx-like DsbG enzyme identifies nucleophilic cysteine hydrogen bonds as key functional determinant.

Ítems similars

• Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant
  per: Lafaye, Céline, et al.
  Publicat: (2016)
• The concerted action of a positive charge and hydrogen bonds dynamically regulates the pK(a) of the nucleophilic cysteine in the NrdH-redoxin family
  per: Van Laer, Koen, et al.
  Publicat: (2014)
• An essential thioredoxin is involved in the control of the cell cycle in the bacterium Caulobacter crescentus
  per: Goemans, Camille V., et al.
  Publicat: (2018)
• NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum Dimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin Reductase
  per: Van Laer, Koen, et al.
  Publicat: (2013)
• Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
  per: Heras, Begoña, et al.
  Publicat: (2004)