Výsledky vyhledávání - "Alycen E. Pond"

Initial characterization of the ferric H175G cytochrome c peroxidase cavity mutant using magnetic circular dichroism spectroscopy: phosphate from the buffer as an axial ligand

Autor: Alycen E. Pond, David B. Goodin, Judy Hirst, John H. Dawson

Publikováno v: International Congress Series. 1233:25-35

Electronic absorption and magnetic circular dichroism (MCD) data are reported for the H175G cavity mutant of yeast cytochrome c peroxidase (H175G CCP) in its ligand-free ferric state at 4 °C under slightly acidic conditions (pH 5.9). Initial analysi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ee9c6bc563b3f915c8e084a317702744
https://doi.org/10.1016/s0531-5131(02)00150-4

Zobrazit plný text záznamu

H93G myoglobin cavity mutant as versatile template for modeling heme proteins: Magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes

Autor: Alycen E. Pond, Mark P. Roach, John H. Dawson

Publikováno v: Biopolymers. 67:200-206

Recent ligand binding and spectroscopic investigations of the myoglobin H93G cavity mutant are reviewed, revealing it to be a versatile template for the preparation of model heme complexes of defined structure. The H93G myoglobin cavity mutant is sho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed563df74a4a7a04c598d22de2931b2b
https://doi.org/10.1002/bip.10087

Zobrazit plný text záznamu

The H93G Myoglobin Cavity Mutant as a Versatile Template for Modeling Heme Proteins: Ferrous, Ferric, and Ferryl Mixed-Ligand Complexes with Imidazole in the Cavity

Autor: Melissa R. Thomas, John H. Dawson, Mark P. Roach, Steven G. Boxer, Alycen E. Pond

Publikováno v: Inorganic Chemistry. 39:6061-6066

One of the difficulties in preparing accurate ambient-temperature model complexes for heme proteins, particularly in the ferric state, has been the generation of mixed-ligand adducts: complexes with different ligands on either side of the heme. The d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f29f592d31c0d97f4265b0acc175b4c4
https://doi.org/10.1021/ic0007198

Zobrazit plný text záznamu

The Role of the Distal and Proximal Protein Environments in Controlling the Ferric Spin State and in Stabilizing Thiolate Ligation in Heme Systems: Thiolate Adducts of the Myoglobin H93G Cavity Mutant

Autor: Steven G. Boxer, Alycen E. Pond, Mark P. Roach, Melissa R. Thomas, John H. Dawson

Publikováno v: Journal of the American Chemical Society. 121:12088-12093

Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by exogenous axial ligands. This approach was pioneer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dcc6046843d32dce06359736068b4364
https://doi.org/10.1021/ja9915504

Zobrazit plný text záznamu

Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH1The reviewing and handling of this manuscript was overseen by a member of the editorial board.1

Autor: John H. Dawson, David B. Goodin, Ann M. English, Masanori Sono, Alycen E. Pond, Duncan E. McRee, Elka A Elenkova

Publikováno v: Journal of Inorganic Biochemistry. 76:165-174

Electronic absorption and magnetic circular dichroism (MCD) spectroscopic data at 4°C are reported for exogenous ligand-free ferric forms of cytochrome c peroxidase (CCP) in comparison with two other histidine-ligated heme proteins, horseradish pero

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::59e5e8ca440e64b5c9c36781e64b4401
https://doi.org/10.1016/s0162-0134(99)00112-9

Zobrazit plný text záznamu

Engineering Cytochrome c Peroxidase into Cytochrome P450: A Proximal Effect on Heme−Thiolate Ligation

Autor: Jeffrey A. Sigman, Yi Lu, John H. Dawson, Alycen E. Pond

Publikováno v: ResearcherID

In an effort to investigate factors required to stabilize heme-thiolate ligation, key structural components necessary to convert cytochrome c peroxidase (CcP) into a thiolate-ligated cytochrome P450-like enzyme have been evaluated and the H175C/D235L

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a16b779d09474c96b62245d7ffe1f0a9
https://doi.org/10.1021/bi990815o

Zobrazit plný text záznamu

Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochromec peroxidase

Autor: Ann M. English, David B. Goodin, John H. Dawson, Elena A. Elenkova, Masanori Sono, Alycen E. Pond

Publikováno v: Biospectroscopy. 5:S42-S52

The addition of exogenous ligands to the ferric and ferrous states of yeast cytochrome c peroxidase (CCP) is investigated with magnetic circular dichroism (MCD) at 4°C to determine the effect the protein environment may exercise on spectral properti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::efcfcfeb9fc0a522d336a85e21373608
https://doi.org/10.1002/(sici)1520-6343(1999)5:5+3.0.co

Zobrazit plný text záznamu

Spectroscopic study of the compound ES and the oxoferryl compound II states of cytochrome c peroxidase: comparison with the compound II of horseradish peroxidase

Autor: Ann M. English, Alycen E. Pond, Masanori Sono, John H. Dawson, Grant S. Bruce

Publikováno v: Inorganica Chimica Acta. :250-255

Magnetic circular dichroism (MCD) spectroscopic data at −30°C are reported for the oxoferryl compound II state of cytochrome c peroxidase (CcP), which was generated by hydrogen peroxide oxidation of ferrous CcP, in comparison with compound ES (an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba000c58363b4f52ea4e7a94ef23abb8
https://doi.org/10.1016/s0020-1693(97)06106-9

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání