Zobrazeno 1 - 10
of 10
pro vyhledávání: '"S F Bowne"'
Autor:
Robert D. Young, S F Bowne
Publikováno v:
The Journal of Chemical Physics. 81:3730-3737
A model of the enthalpy barrier between the heme pocket and heme iron is proposed for the recombination of small ligands to heme proteins after flash photolysis. The model is based on the concept of conformational substates as developed by Frauenfeld
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b439f09e3b98aa5ae4ba1d909bd921b
https://doi.org/10.1063/1.448124
https://doi.org/10.1063/1.448124
Publikováno v:
Journal of Molecular Biology. 194:299-312
The recombination of carbon monoxide to isoenzymes A2 and C of horseradish peroxidase (HRP) was studied as a function of temperature (2 to 320 K) and pH (5 to 8.3) with flash photolysis and infrared difference absorption. At low temperatures three ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cc385f12cf605c0cd3ca416daae01cc
https://doi.org/10.1016/0022-2836(87)90377-9
https://doi.org/10.1016/0022-2836(87)90377-9
Autor:
Lou Reinisch, A. H. Reynolds, J D McDonald, S F Bowne, D. Beece, P. P. Moh, Hans Frauenfelder, K T Yue, E. Shyamsunder, W Doster, D. Good, L. Eisenstein, J. O. Alben, M. C. Marden
Publikováno v:
Proceedings of the National Academy of Sciences. 79:3744-3748
We have studied the infrared spectra of the bound and photodissociated states of Mb-12CO and Mb-13CO from 5.2 to 300 K. The absorbance peaks seen between 1800 and 2200 cm-1 correspond to CO stretching vibrations. In the bound state of Mb-12CO, the kn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bfeae7cb14aead1eaf3c028fb67edc8
https://doi.org/10.1073/pnas.79.12.3744
https://doi.org/10.1073/pnas.79.12.3744
Autor:
J. Czégé, S. F. Bowne, Hans Frauenfelder, K. T. Yue, M. C. Marden, Lou Reinisch, D. Beece, D. Good, L. Eisenstein, J. Marque, Pál Ormos
Publikováno v:
Photochemistry and Photobiology. 33:517-522
— We study the effect of solvent viscosity on the kinetics of the photocycle of bacteriorhodopsin (bR) from Halobacterium halobium. Solvent viscosity is altered by changing the glycerol concentration from 20 to 80% glycerol by volume. The kinetics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8263f4171bc7cf3857b642ed0e90274e
https://doi.org/10.1111/j.1751-1097.1981.tb05454.x
https://doi.org/10.1111/j.1751-1097.1981.tb05454.x
Autor:
S. F. Bowne, M. C. Marden, Lou Reinisch, F Stetzkowski, L. Eisenstein, E. Shyamsunder, W Doster, Ramaprasad Banerjee, D. Beece, Hans Frauenfelder
Publikováno v:
Journal of Biological Chemistry. 260:8803-8809
The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad8113f23a99e5a340104ece5539f580
https://doi.org/10.1016/s0021-9258(17)39423-1
https://doi.org/10.1016/s0021-9258(17)39423-1
Autor:
S. F. Bowne, P. P. Moh, M. C. Marden, Lou Reinisch, K. T. Yue, L. Eisenstein, D. Beece, Hans Frauenfelder, A. H. Reynolds, D. Good, J. O. Alben
Publikováno v:
Physical Review Letters. 44:1157-1160
The intramolecular binding of carbon monoxide ($^{13}\mathrm{C}$$^{16}\mathrm{O}$/$^{12}\mathrm{C}$$^{16}\mathrm{O}$ and $^{12}\mathrm{C}$$^{18}\mathrm{O}$/$^{12}\mathrm{C}$$^{16}\mathrm{O}$ mixtures) to myoglobin at 20 and 60 K is observed with time
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::37340421bc4db1135167093cb14e5495
https://doi.org/10.1103/physrevlett.44.1157
https://doi.org/10.1103/physrevlett.44.1157
Autor:
L. Eisenstein, Kwok To Yue, D. Beece, S. F. Bowne, W Doster, Ernesto E. DiIorio, Lou Reinisch, E. Shyamsunder, Hans Frauenfelder, K. H. Winterhalter
Publikováno v:
Biochemistry. 21:4831-4839
The recombination after flash photolysis of dioxygen and carbon monoxide with sperm whale myoglobin (Mb), and separated beta chains of human hemoglobin (beta A) and hemoglobin Zürich (beta ZH), has been studied as a function of pH and temperature fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd3f3e3c6dff88ae12d9fd62bf1e9d0e
https://doi.org/10.1021/bi00263a001
https://doi.org/10.1021/bi00263a001
Autor:
F, Stetzkowski, R, Banerjee, M C, Marden, D K, Beece, S F, Bowne, W, Doster, L, Eisenstein, H, Frauenfelder, L, Reinisch, E, Shyamsunder
Publikováno v:
The Journal of biological chemistry. 260(15)
The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::28eaf1b1a9ffdb725e8fa096a6888255
https://pubmed.ncbi.nlm.nih.gov/4040516
https://pubmed.ncbi.nlm.nih.gov/4040516
Autor:
E. Shyamsunder, S F Bowne, Heinrich Roder, Todd B. Sauke, Hans Frauenfelder, Joel Berendzen, M B Weissman
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 81(8)
The magnetic susceptibility of photodissociated carbon monoxy myoglobin has been measured over the temperature range from 1.7 to 25 K at 10 and 50 kG with a superconducting susceptometer. The spin and the crystal field parameters of the iron ion were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd54a9432f553d46fefd3df7c3d07340
https://pubmed.ncbi.nlm.nih.gov/6585802
https://pubmed.ncbi.nlm.nih.gov/6585802
Autor:
Joel Berendzen, Robert D. Young, Icko Iben, E. Shyamsunder, Hans Frauenfelder, Todd B. Sauke, S F Bowne, Anjum Ansari
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 82(15)
After photodissociation of carbon monoxide bound to myoglobin, the protein relaxes to the deoxy equilibrium structure in a quake-like motion. Investigation of the proteinquake and of related intramolecular equilibrium motions shows that states and mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12c84711d75d3a442817f0cdc3d0a403
https://pubmed.ncbi.nlm.nih.gov/3860839
https://pubmed.ncbi.nlm.nih.gov/3860839