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Comment
. 2009 Feb 4;28(3):169-70.
doi: 10.1038/emboj.2008.293.

A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway

Robert B Freedman  1
Affiliations
Comment

A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway

Robert B Freedman. EMBO J. .
No abstract available

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Figures

Figure 1
Figure 1
(A) In the absence of a reduced substrate, PDI and the FAD and inner disulphide redox centres of Ero1α are oxidised, the regulatory C94–C131 disulphide forms and the glutathione buffer is shifted towards GSSG. (B) In the presence of a reduced substrate, some PDI is converted to the reduced form, which reduces the regulatory disulphide; reducing equivalents flow from substrate protein to O2, all redox centres interconvert between the oxidised and reduced state and the glutathione buffer shifts towards GSH.
See this image and copyright information in PMC

Comment on

References

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