Asset Details
Do you wish to reserve the book?
Solution Structure and Dynamics of the Complex between Cytochrome c and Cytochrome c Peroxidase Determined by Paramagnetic NMR
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Solution Structure and Dynamics of the Complex between Cytochrome c and Cytochrome c Peroxidase Determined by Paramagnetic NMR
Do you wish to request the book?
Solution Structure and Dynamics of the Complex between Cytochrome c and Cytochrome c Peroxidase Determined by Paramagnetic NMR
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Solution Structure and Dynamics of the Complex between Cytochrome c and Cytochrome c Peroxidase Determined by Paramagnetic NMR
2006
Overview
The physiological complex of yeast cytochrome c peroxidase and iso-l-cytochrome c is a paradigm for biological electron transfer. Using paramagnetic NMR spectroscopy, we have determined the conformation of the protein complex in solution, which is shown to be very similar to that observed in the crystal structure [Pelletier H, Kraut J (1992) Science 258:1748-1755]. Our results support the view that this transient electron transfer complex is dynamic. The solution structure represents the dominant protein-protein orientation, which, according to our estimates, is occupied for >70% of the lifetime of the complex, with the rest of the time spent in the dynamic encounter state. Based on the observed paramagnetic effects, we have delineated the conformational space sampled by the protein molecules during the dynamic part of the interaction, providing experimental support for the theoretical predictions of the classical Brownian dynamics study [Northrup SH, Boles JO, Reynolds JCL (1988) Science 241:67-70]. Our findings corroborate the dynamic behavior of this complex and offer an insight into the mechanism of the protein complex formation in solution.
Publisher
National Academy of Sciences,National Acad Sciences
