Recombinant proteins Redox

The replacement of native haem with metal-substituted porphyrin can be performed in two ways. In the first, iron ions are removed from the protein by treating native protein with anhydrous HF, followed by insertion of the appropriate metal to metal-free protein [57-59]. In the second, haem is removed either chemically or by recombination (preparing a proper recombinant protein), and then protein is reconstituted with metal-substituted porphyrins [60-64]. The Zn-substituted metal-loproteins such as cytochrome c [65-67], myoglobin [59,61, 62, 64, 68, 69], and haemoglobin [64, 68,70] have been extensively used to study photoinduced ET (PET) between modified proteins and their physiological redox partners. Interestingly, in haemoglobin with a and /3 subunits it was possible to determine ET parameters for... 

A correct folding of recombinant proteins is regulated by the redox potential of the outer compartments and performed by foldases. These catalyse disulfide bond formation and peptidyl-proline isomerization, prevent protein a regation in inclusion bodies and hamper the proteolysis by cytoplasmic enzymes. The coexptession of eukaryotic foldases leads to an increased yield of eukaryotic recombinant proteins in E. colif Moreover, the supply of reduced glutathione generates favourable environmental conditions for carrying out a correct folding in the periplasm. ... 

D., and Gasser, B. (2014) Engineering of protein folding and secretion-strategies to overcome bottlenecks for efficient production of recombinant proteins. Antioxid. Redox Signal., 21, 414—437. 

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