Search Results - "Satterlee, J.D"

Species-specific differences in covalently crosslinked complexes of yeast cytochrome c peroxidase with horse and yeast iso-1 ferricytochromes c by Moench, S J, Erman, J E, Satterlee, J D

“…1. The results of chemically crosslinking yeast cytochrome c peroxidase with both horse and yeast iso-1 ferricytochromes c have been studied by a combination…”
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Proton NMR assignments of heme contracts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects by Satterlee, J.D., Erman, J.E.

“…Proton NMR assignments of the heme pocket and catalytically relevant amino acid protons have been accomplished for cyanide-ligated yeast cytochrome c…”
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Assignment of 1H and 13C hyperfine-shifted resonances for tuna ferricytochrome c by Sukits, S.F., Satterlee, J.D.

“…Tuna ferricytochrome c has been used to demonstrate the potential for completely assigning 1H and 13C strongly hyperfine-shifted resonances in metalloprotein…”
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Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c by Yi, Qian, Erman, James E., Satterlee, James D.

“…Noncovalent complexes of cyanide-ligated cytochrome c peroxidase with horse ferricytochrome c and yeast isozyme-1 ferricytochrome c have been formed in 10 mM…”
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Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235 yields Asn-235 mutant by Satterlee, J.D., Erman, J.E., Mauro, J.M., Kraut, J.

“…Proton NMR spectra of cytochrome c peroxidase (CcP) isolated from yeast (wild type) and two Escherichia coli expressed proteins, the parent expressed protein…”
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Anomalously slow cyanide binding to Glycera dibranchiata monomer methemoglobin component II: implication for the equilibrium constant by Mintorovitch, Jan, Satterlee, James D

“…In comparison to sperm whale metmyoglobin, metleghemoglobin a, methemoglobins, and heme peroxidases, the purified Glycera dibranchiata monomer methemoglobin…”
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Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c by Satterlee, J.D., Moench, S.

“…Proton hyperfine resonance assignments for cytochromes c from several species are currently being successfully pursued by several laboratories. These efforts…”
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Ferricytochrome c binding induces detectable proton NMR shift changes in cytochrome c peroxidase-CN by Yi, Qian, Erman, James E, Satterlee, James D

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One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isoenzyme-1 ferricytochrome c by Busse, S.C. (New Methods Research Inc., Syracuse, NY), Moench, S.J, Satterlee, J.D

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Proton NMR comparison of the Saccharomyces cerevisiae ferricytochrome c isozyme-1 monomer and covalent disulfide dimer by Moench, S J, Satterlee, J D

“…Proton NMR studies of Saccharomyces cerevisiae (bakers yeast) isozyme-1 monomer and dimer ferricytochrome c have been carried out. The dimer is formed via a…”
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One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c by Busse, S.C., Moench, S.J., Satterlee, J.D.

“…The effect of S-methylating cysteine-102 (cys-102) (SH---SSCH3) of yeast isozyme-1 (iso-1) ferricytochrome c has been studied using proton NMR spectroscopy…”
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Deuterium isotope effect on the heme-coordinated CO vibration band of ferrous cytochrome c peroxidase-CO by SATTERLEE, J. D, ERMAN, J. E

“…The question of distal effects as mediators of ligand binding in heme proteins has resulted in efforts to discern the role of the distal histidine at position…”
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effect of the Asn82 to Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy by Satterlee, J.D, Alam, S.L, Mauro, J.M, Erman, J.E, Poulos, T.L

“…Proton NMR studies of the mutant of baker's yeast cytochrome c peroxidase-cyanide with the Asn 82 leads to Asp mutation ([N82D]cytochrome c peroxidase-CN) are…”
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Assignment of selected hyperfine proton NMR resonances in the met forms of Glycera dibranchiata monomer hemoglobins and comparisons with sperm whale metmyoglobin by Constantinidis, Ioannis, Satterlee, James D, Pandey, Ravindra K, Leung, Hiu Kwong, Smith, Kevin M

“…This work indicates a high degree of purity for our preparations of all three of the primary Glycera dibranchiata monomer hemoglobins and details assignments…”
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Aggregation of uroporphyrin I and its metal derivatives in aqueous solution: Raman difference spectroscopy and absorption spectroscopy by Shelnutt, J. A, Dobry, M. M, Satterlee, J. D

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Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase by Satterlee, J D, Erman, J E

“…Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase compound I, drastically alters…”
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Studies of urohemin I in aqueous solution. Thermodynamics of self-association and electronic properties of two species detected by proton NMR spectroscopy by Satterlee, James D, Shelnutt, John A

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Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect by Satterlee, J D, Avizonis, D Z, Moench, S J

“…Yeast cytochrome c isozyme 2 is one of two cytochrome c isozymes which are found in yeast mitochondria. Unlike isozyme 1, which can dimerize in vitro due to a…”
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