Zobrazeno 1 - 10
of 211
pro vyhledávání: '"D. Satterlee"'
Autor:
Gregory L. Helms, James D. Satterlee
Publikováno v:
Magnetic Resonance in Chemistry. 51:222-229
Metalloproteins are a category of biomolecules in which the metal site is usually the locus of activity or function. In many cases, the metal ions are paramagnetic or have accessible paramagnetic states, many of which can be studied using NMR spectro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::67cb16d24b71a346c56e047018acb0f4
https://doi.org/10.1002/mrc.3929
https://doi.org/10.1002/mrc.3929
Autor:
Xuhong Zhang, Jerry L. Dallas, Kevin M. Smith, Li-Hua Ma, Michihiko Sato, Dungeng Peng, Gerd N. La Mar, James D. Satterlee
Publikováno v:
Biochemistry. 50:8823-8833
Heme oxygenase (HO), from the pathogenic bacterium N. meningitidis(NmHO), which secures host iron, shares many properties with mammalian HOs but also exhibits some key differences. The crystal structure appears more compact, and the crystal-undetecte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4c212d614dfaacf0a3dbf03a451cf0d
https://doi.org/10.1021/bi200978g
https://doi.org/10.1021/bi200978g
Autor:
James D. Satterlee
Publikováno v:
Journal of Inorganic Biochemistry. 105:609-615
Nine recombinant FixL heme domains from Bradyrhizobium japonicum previously were shown to exhibit mass instability independent of many environmental factors (J.D. Satterlee, C. Suquet, A. Bidwai, J. Erman, L. Schwall, R. Jimenez, Biochemistry 47 (200
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77b0c68e7a66dd6c845eeac409e00951
https://doi.org/10.1016/j.jinorgbio.2011.01.015
https://doi.org/10.1016/j.jinorgbio.2011.01.015
Autor:
Anil K. Bidwai, Linda R. Schwall, James D. Satterlee, Christine Suquet, Ralph Jimenez, James E. Erman
Publikováno v:
Biochemistry. 47:1540-1553
Several recombinant Bradyrhizobium japonicum FixL heme domains (BjFixLH) have been characterized and their temporal mass stabilities assessed by MALDI-TOF mass spectrometry. The intact heme domains all bound heme and gave normal UV-visible spectra, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24a0523abe8d4e9541cdf6a6ac995c29
https://doi.org/10.1021/bi701672m
https://doi.org/10.1021/bi701672m
Publikováno v:
FEBS Letters. 581:4512-4518
Here we report the results of transient absorption and photoacoustic calorimetry studies of CO photodissociation from the heme domain of the bacterial oxygen sensor HemAT-Bs. The results indicate that CO photolysis is accompanied by an overall DeltaH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5189fe208e38ba3096fd4b51759d644
https://doi.org/10.1016/j.febslet.2007.08.031
https://doi.org/10.1016/j.febslet.2007.08.031
Publikováno v:
Biochemistry. 45:13875-13888
Solution 1H NMR has been used to characterize the active site molecular and electronic structure of the cyanide-inhibited 2,4-dimethyldeuterohemin complex of the heme oxygenase from Neisseria meningitidis (NmHO) with respect to the mode of interactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f059ae85b53e87553af73b95150192d
https://doi.org/10.1021/bi061747q
https://doi.org/10.1021/bi061747q
Autor:
Martin L. Pall, James D. Satterlee
Publikováno v:
Annals of the New York Academy of Sciences. 933:323-329
Various types of evidence implicate nitric oxide and an oxidant, possibly peroxynitrite, in MCS and chemical intolerance (CI). The positive feedback loops proposed earlier for CFS may explain the chronic nature of MCS (CI) as well as several of its o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e52ed5e5d672c69e93b846f8d816f5db
https://doi.org/10.1111/j.1749-6632.2001.tb05836.x
https://doi.org/10.1111/j.1749-6632.2001.tb05836.x
Publikováno v:
Biochemistry. 44:10028-10036
Using transient absorption spectroscopy and photoacoustic calorimetry (PAC), we have characterized carbon monoxide photodissociation and rebinding to two forms of the heme domain of Bradyrhizobium japonicum FixL. Transient absorption results for the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9a2d20509a74becc30dc454e3533aa3
https://doi.org/10.1021/bi047369b
https://doi.org/10.1021/bi047369b
Autor:
Alexandra Sauer-Masarwa, Hiroshi Fujii, Daryle H. Busch, Brian M. Hoffman, James D. Satterlee, Roman Davydov
Publikováno v:
Journal of the American Chemical Society. 125:16340-16346
Cryoreduction of the [FeO2]6 (n = 6 is the number of electrons in 3d orbitals on Fe and pi* orbitals on O2) dioxygen-bound ferroheme through irradiation at 77 K generates an [FeO2]7 reduced oxy-heme. Numerous investigations have examined [FeO2]7 cent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::843e8bbc4116b165cc92401d953ef346
https://doi.org/10.1021/ja037037e
https://doi.org/10.1021/ja037037e