Zobrazeno 1 - 10
of 31
pro vyhledávání: '"J. T. Sage"'
Autor:
Paul M. Champion, Xiong Ye, J. T. Sage, Georgi Georgiev, Anchi Yu, Wenxiang Cao, Dan Ionascu, Florin Gruia
Publikováno v:
Journal of the American Chemical Society. 127:5854-5861
The rebinding kinetics of CO to protoheme (FePPIX) in the presence and absence of a proximal imidazole ligand reveals the magnitude of the rebinding barrier associated with proximal histidine ligation. The ligation states of the heme under different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d88784478a2ce85c87b029cc206b3173
https://doi.org/10.1021/ja042365f
https://doi.org/10.1021/ja042365f
Autor:
Xiong Ye, Georgi Georgiev, J. T. Sage, Svitlana Y. Berezhna, Wenxiang Cao, Paul M. Champion, Wei Wang, and Andrey A. Demidov, Theodore Sjodin
Publikováno v:
Biochemistry. 43:7017-7027
We use laser flash photolysis and time-resolved Raman spectroscopy of CO-bound heme complexes to study proximal and distal influences on ligand rebinding kinetics. We report kinetics of CO rebinding to microperoxidase (MP) and 2-methylimidazole ligat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d614b651b11e56433763f188bc104002
https://doi.org/10.1021/bi0497291
https://doi.org/10.1021/bi0497291
Autor:
Wolfgang Sturhahn, Stephen M. Durbin, J. T. Sage, A. Roth, Earl W. Prohofsky, Brajesh K. Rai, E. Ercan Alp, M. K. Ellison, W. R. Scheidt
Publikováno v:
Journal of the American Chemical Society. 125:6927-6936
Detailed Fe vibrational spectra have been obtained for the heme model complex [Fe(TPP)(CO)(1-MeIm)] using a new, highly selective and quantitative technique, Nuclear Resonance Vibrational Spectroscopy (NRVS). This spectroscopy measures the complete v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::becd5cac003c7b8e5f85811534c4fef4
https://doi.org/10.1021/ja028219w
https://doi.org/10.1021/ja028219w
Autor:
Stephen M. Durbin, E. Ercan Alp, P. M. Champion, W. R. Scheidt, J. T. Sage, C Paxson, Wolfgang Sturhahn, Graeme R. A. Wyllie
Publikováno v:
Journal of Physics: Condensed Matter. 13:7707-7722
For many years, Mossbauer spectroscopy has been applied to measure recoilless absorption of x-ray photons by nuclei. Recently, synchrotron radiation sources have enabled the observation of weaker features separated from the recoilless resonance by th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afce12e52685a351ad842cd8f714f4b0
https://doi.org/10.1088/0953-8984/13/34/315
https://doi.org/10.1088/0953-8984/13/34/315
Autor:
Jee W, J. T. Sage
Publikováno v:
Journal of Molecular Biology. 274:21-26
We use polarized IR absorption on single crystals to determine the orientation of carbon monoxide bound at the active site of myoglobin, and conclude that the C-O bond lies approximately 7 degrees from the normal to the mean plane of the heme. This r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a3cc51e1c8eb2cc1515cee579f40b4b
https://doi.org/10.1006/jmbi.1997.1367
https://doi.org/10.1006/jmbi.1997.1367
Autor:
Alexander Barabanschikov, Mary K. Ellison, Wolfgang Sturhahn, Jiyong Zhao, Marek Z. Zgierski, Scheidt Wr, Chuanjiang Hu, J. T. Sage, E. E. Alp
Nuclear resonance vibrational spectra have been obtained for six five-coordinate imidazole-ligated iron(II) porphyrinates, [Fe(Por)(L)] (Por = tetraphenylporphyrinate, octaethylporphyrinate, tetratolylporphyrinate, or protoporphyrinate IX and L = 2-m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94ffc56a03cb2f913c3f55c2e9607542
https://nrc-publications.canada.ca/eng/view/object/?id=ce12c5cd-3678-4db7-844e-85df7167ce7f
https://nrc-publications.canada.ca/eng/view/object/?id=ce12c5cd-3678-4db7-844e-85df7167ce7f
Publikováno v:
Science. 266:629-632
Femtosecond laser pulses, resonant with Soret band of the nitric oxide complex of myoglobin (MbNO), were used to probe coherent, low-frequency nuclear motion of the heme group after photolysis. Distinct oscillations with periods of 430 and 150 femtos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29372955c159cde1b18f221ec00bf64c
https://doi.org/10.1126/science.7939716
https://doi.org/10.1126/science.7939716
Publikováno v:
The Journal of Chemical Physics. 97:3214-3227
We discuss the technique of resonance Raman saturation spectroscopy and present experimental results that probe relaxation processes in heme proteins following electronic excitation in the Soret band. The observable relaxation time scales are limited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4e24528e3b7cc5a872904c868af0814
https://doi.org/10.1063/1.463008
https://doi.org/10.1063/1.463008
Publikováno v:
Scopus-Elsevier
ResearcherID
ResearcherID
Recently, there has been interest in determining the conditions under which the iron-histidine bond ruptures in myoglobin at low pH, so that the effect of proximal heme ligation can be studied. A 220-cm-1 Raman mode, assigned to iron-histidine stretc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56c11949b9778afd972530a6b802d9d5
Publikováno v:
Journal of Molecular Biology. 224:207-215
We present evidence that the structure of carbonmonoxy myoglobin crystals can be altered by lowering the pH. This structural change is monitored by the characteristic Fe-CO Raman modes at 508 and 491 cm-1 and is thought to involve a localized distal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::916133dd8bd4127f7e076ca52d255d8d
https://doi.org/10.1016/0022-2836(92)90584-7
https://doi.org/10.1016/0022-2836(92)90584-7