Abstract
Recent picosecond transient absorption studies1 show that the yield of geminate rebinding is sensitive to protein structure. Picosecond transient Raman studies2 reveal that over the time course (Շ ≃ 200 ps) of the geminate rebinding, the effective tertiary structure about the heme is not relaxing. The results of this study also imply strong coupling among the elements of tertiary structure that control both the frequency of iron-proximal histidine stretching motion and the ligand binding properties of the heme. These findings and conclusions are used to further develop a working model in which reactivity and structure about the heme are controlled by an effective tertiary structure associated with what Karplus and co-workers3call an "allosteric core" comprised of the heme, the proximal histidine (F-8), a portion of the F-helix and the α1-β2 interface.
Original language | English (US) |
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Pages (from-to) | 8-14 |
Number of pages | 7 |
Journal | Proceedings of SPIE - The International Society for Optical Engineering |
Volume | 533 |
DOIs | |
State | Published - Apr 3 1985 |
Externally published | Yes |
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Condensed Matter Physics
- Computer Science Applications
- Applied Mathematics
- Electrical and Electronic Engineering