Search Results - Woehl, Eilika

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  1. 1
    Protein architecture, dynamics and allostery in tryptophan synthase channeling

    Protein architecture, dynamics and allostery in tryptophan synthase channeling by Pan, Peng, Woehl, Eilika, Dunn, Michael F.

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  2. 2
    Monovalent Metal Ions Play an Essential Role in Catalysis and Intersubunit Communication in the Tryptophan Synthase Bienzyme Complex

    Monovalent Metal Ions Play an Essential Role in Catalysis and Intersubunit Communication in the Tryptophan Synthase Bienzyme Complex by Woehl, Eilika U, Dunn, Michael F

    Published in Biochemistry (Easton)
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  3. 3
    Allosteric linkages between .beta.-site covalent transformations and .alpha.-site activation and deactivation in the tryptophan synthase bienzyme complex

    Allosteric linkages between .beta.-site covalent transformations and .alpha.-site activation and deactivation in the tryptophan synthase bienzyme complex by Leja, Catherine A, Woehl, Eilika U, Dunn, Michael F

    Published in Biochemistry (Easton)
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  4. 4
    Kinetic Isotope Effects as a Probe of the β-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase

    Kinetic Isotope Effects as a Probe of the β-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase by Hwang, Chi-Ching, Woehl, Eilika U, Minter, David E, Dunn, Michael F, Cook, Paul F

    Published in Biochemistry (Easton)
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  5. 5
    Mechanisms of Monovalent Cation Action in Enzyme Catalysis:  The Tryptophan Synthase α-, β-, and αβ-Reactions

    Mechanisms of Monovalent Cation Action in Enzyme Catalysis:  The Tryptophan Synthase α-, β-, and αβ-Reactions by Woehl, Eilika, Dunn, Michael F

    Published in Biochemistry (Easton)
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  6. 6
    Mechanisms of Monovalent Cation Action in Enzyme Catalysis:  The First Stage of the Tryptophan Synthase β-Reaction

    Mechanisms of Monovalent Cation Action in Enzyme Catalysis:  The First Stage of the Tryptophan Synthase β-Reaction by Woehl, Eilika, Dunn, Michael F

    Published in Biochemistry (Easton)
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  7. 7
    The roles of Na + and K + in pyridoxal phosphate enzyme catalysis

    The roles of Na + and K + in pyridoxal phosphate enzyme catalysis by Woehl, Eilika U., Dunn, Michael F.

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  8. 8
    Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants

    Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants by Choudhury, K, Sundaramoorthy, M, Hickman, A, Yonetani, T, Woehl, E, Dunn, M F, Poulos, T L

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  9. 9
    Formation of the α-Aminoacrylate Intermediate Limits the Overall Reaction Catalyzed by O-Acetylserine Sulfhydrylase

    Formation of the α-Aminoacrylate Intermediate Limits the Overall Reaction Catalyzed by O-Acetylserine Sulfhydrylase by Woehl, Eilika U., Tai, Chia-Hui, Dunn, Michael F., Cook, Paul F.

    Published in Biochemistry (Easton)
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  10. 10
    Substitution of pyridoxal 5'-phosphate in the O-acetylserine sulfhydrylase from Salmonella typhimurium by cofactor analogs provides a test of the mechanism proposed for formation of the alpha-aminoacrylate intermediate

    Substitution of pyridoxal 5'-phosphate in the O-acetylserine sulfhydrylase from Salmonella typhimurium by cofactor analogs provides a test of the mechanism proposed for formation o... by Cook, P F, Tai, C H, Hwang, C C, Woehl, E U, Dunn, M F, Schnackerz, K D

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  11. 11
    Substitution of Pyridoxal 5′-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides a Test of the Mechanism Proposed for Formation of the α-Aminoacrylate Intermediate

    Substitution of Pyridoxal 5′-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides a Test of the Mechanism Proposed for Formation... by Paul F. Cook, Chia-Hui Tai, Chi-Ching Hwang, Eilika U. Woehl, Michael F. Dunn, Klaus D. Schnackerz

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