Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Lidia B. Vitello"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854:919-929
Imidazole binding to three apolar distal heme pocket mutants of yeast cytochrome c peroxidase (CcP) has been investigated between pH4 and 8. The three CcP variants have Arg-48, Trp-51, and His-52 mutated to either all alanine, CcP(triAla), all valine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e49bcb81db593de5364068854973edb
https://doi.org/10.1016/j.bbapap.2015.04.014
https://doi.org/10.1016/j.bbapap.2015.04.014
Autor:
James E. Erman, Naw May Pearl, Erik M. Alberts, Timothy Jacobson, Kathy Bujarska, Allen Kou, Meka Francis, Lidia B. Vitello
Publikováno v:
Biochemistry. 54:4845-4854
Previously, we constructed, expressed, and purified 46 charge-reversal mutants of yeast cytochrome c peroxidase (CcP) and determined their electronic absorption spectra, their reaction with H2O2, and their steady-state catalytic properties [ Pearl ,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64b350b056f2a4f19bdf9638ebe8279a
https://doi.org/10.1021/acs.biochem.5b00686
https://doi.org/10.1021/acs.biochem.5b00686
Publikováno v:
Biochemical and Biophysical Research Communications. 443:200-204
Ferric heme proteins bind weakly basic ligands and the binding affinity is often pH dependent due to protonation of the ligand as well as the protein. In an effort to find a small, neutral ligand without significant acid/base properties to probe liga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c611db5da497b9d44ac6371e53c6f49
https://doi.org/10.1016/j.bbrc.2013.11.084
https://doi.org/10.1016/j.bbrc.2013.11.084
Publikováno v:
Biochemistry. 46:8263-8272
Fifteen single-site charge-reversal mutations of yeast cytochrome c peroxidase (CcP) have been constructed in order to determine the effect of localized charge on the catalytic properties of the enzyme. The mutations are located on the front face of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ec781f003b981fe12717486d623e1d2
https://doi.org/10.1021/bi700623u
https://doi.org/10.1021/bi700623u
Equilibrium and kinetic properties of cyanide and imidazole binding to the heme domains of Sinorhizobium meliloti and Bradyrhizobium japonicum FixL (SmFixLH and BjFixLH) have been investigated between pH 5 and 11. KD determinations were made at integ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65ceff509171641880ea4a4f7ba89f4b
https://europepmc.org/articles/PMC4690814/
https://europepmc.org/articles/PMC4690814/
Autor:
Lidia B. Vitello, Siddartha Nakani, James E. Erman, Thanarat Viriyakul, Robert Alexander Mitchell
Publikováno v:
Biochemistry. 45:9887-9893
A covalent complex between recombinant yeast iso-1-cytochrome c and recombinant yeast cytochrome c peroxidase (rCcP), in which the crystallographically defined cytochrome c binding site [Pelletier, H., and Kraut, J. (1992) Science 258, 1748-1755] is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c42a77dff2d3f60249ca21db1f4e87e8
https://doi.org/10.1021/bi060586n
https://doi.org/10.1021/bi060586n
Autor:
Timothy Jacobson, Joy Williamson, James E. Erman, Anthony Wasilewski, Janet Felesik, Lidia B. Vitello
Publikováno v:
Archives of Biochemistry and Biophysics. 422:125-136
Yeast cytochrome c peroxidase (CcP) and horse metmyoglobin (Mb) bind HN 3 with similar affinities at 25 °C. The pH-independent equilibrium association constants for formation of the CcP · HN 3 and Mb · HN 3 complexes are (1.05 ± 0.06) × 10 5 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96066bdd79e095b253831cf7ea7a906d
https://doi.org/10.1016/j.abb.2003.12.016
https://doi.org/10.1016/j.abb.2003.12.016
Publikováno v:
Biochemistry. 42:10764-10771
Cyanide binding to a cytochrome c peroxidase (CcP) variant in which the distal histidine has been replaced by a leucine residue, CcP(H52L), has been investigated as a function of pH using spectroscopic, equilibrium, and kinetic methods. Between pH 4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7fe837357c6070f17f808007151bbcd
https://doi.org/10.1021/bi034632k
https://doi.org/10.1021/bi034632k
Autor:
Lidia B. Vitello, James E. Erman
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1597:193-220
Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme that catalyzes the reduction of hydrogen peroxide to water by ferrocytochrome c. It was the first heme enzyme to have its crystallographic structure determined and, as a consequence, has p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c7c8f5ed514a48c19868717473f305c
https://doi.org/10.1016/s0167-4838(02)00317-5
https://doi.org/10.1016/s0167-4838(02)00317-5
Publikováno v:
Biochemistry. 38:15647-15652
The rate of the reaction between p-nitroperoxybenzoic acid and cytochrome c peroxidase (CcP) has been investigated as a function of pH and ionic strength. The pH dependence of the reaction between CcP and peracetic acid has also been determined. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d7088aefa76549772e3ed5d09cb9c44
https://doi.org/10.1021/bi991497w
https://doi.org/10.1021/bi991497w