... redox potential thiol-disulfide exchange A family of proteins, collectively termed the protein disulfide isomerases (PDIs), is responsible for formation of correct disulfides in proteins entering the secretory pathway. This protein family is characterized by the presence of one or more domains...

...) uses a monothiol mechanism to reduce the hSOD1 disulfide, and the GSH/hGrx1 system reduces ALS mutant SOD1 at a faster rate than WT (wild-type) hSOD1. However, redox potential measurements demonstrate that the thermodynamic stability of the disulfide is not consistently lower in ALS mutants compared...

... a redox change in the C-terminal domain Cys 186 –Cys 209 disulfide bond. The redox potential of the bond, the spacing of the reduced cysteine thiols and their oxidation by TF activators was investigated to test the involvement of the dithiol/disulfide in TF activation. A standard redox potential of −278...

... of chimaeric CPRs in solution. Results of the present study highlight the role of the linker and connecting domain in the recognition at the interfaces between the catalytic domains and the impact of interdomain interactions on the redox potentials of the flavins, the internal electron-transfer efficiency...

... 2009 17 6 2009 17 6 2009 © The Authors Journal compilation © 2009 Biochemical Society 2009 cytochrome c oxidase haem mitochondrion near infrared spectroscopy redox potential steady-state enzyme kinetics We have therefore re-examined the behaviour of the isolated...

... exhibits a relatively high redox potential (+131 mV) and the C154A mutant displays a lower potential (+70 mV), while the H94A mutant displays a relatively high potential of approximately +164 mV. The results show that a high redox potential is not the only prerequisite to ensure efficient catalysis...

... between the gold surface and the T1 copper site progresses through the T2 copper site. From EPR measurements and electrochemical data it is proposed that the redox potential of the T2 site for high-potential ‘blue’ laccase is equal to about 400 mV versus NHE (normal hydrogen electrode) at pH 6.5...

... of holo-X, yielding holo-sGDH, caused not only stabilization of the semiquinone form of PQQ but also a negative shift (of 26.5mV) of the two-electron redox potential, indicating that the effect of Ca 2+ is stronger on the oxidized than on the reduced PQQ. Combining these data with the observations...