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Nitrogenase and biological nitrogen fixation
Nitrogenase and biological nitrogen fixation
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Nitrogenase and biological nitrogen fixation

Kim, Jongsun ; Rees, Douglas C

Biochemistry (Easton), 1994-01, Vol.33 (2), p.389-397 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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2
Mechanism for the Desulfurization of L-Cysteine Catalyzed by the nifS Gene Product
Mechanism for the Desulfurization of L-Cysteine Catalyzed by the nifS Gene Product
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Mechanism for the Desulfurization of L-Cysteine Catalyzed by the nifS Gene Product

Zheng, Limin ; White, Robert H ; Cash, Valerie L ; Dean, Dennis R

Biochemistry (Easton), 1994-04, Vol.33 (15), p.4714-4720 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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3
Kinetic and Calcium-Binding Properties of Three Calcium-Dependent Protein Kinase Isoenzymes from Soybean
Kinetic and Calcium-Binding Properties of Three Calcium-Dependent Protein Kinase Isoenzymes from Soybean
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Kinetic and Calcium-Binding Properties of Three Calcium-Dependent Protein Kinase Isoenzymes from Soybean

Lee, Jung-Youn ; Yoo, Byung-Chun ; Harmon, Alice C

Biochemistry (Easton), 1998-05, Vol.37 (19), p.6801-6809 [Periódico revisado por pares]

United States: American Chemical Society

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4
Kinase Activity of Oxygen Sensor FixL Depends on the Spin State of Its Heme Iron
Kinase Activity of Oxygen Sensor FixL Depends on the Spin State of Its Heme Iron
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Kinase Activity of Oxygen Sensor FixL Depends on the Spin State of Its Heme Iron

Gilles-Gonzalez, Marie A ; Gonzalez, Gonzalo ; Perutz, Max F

Biochemistry (Easton), 1995-01, Vol.34 (1), p.232-236 [Periódico revisado por pares]

United States: American Chemical Society

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5
Crystal Structures of Soybean .beta.-Amylase Reacted with .beta.-Maltose and Maltal: Active Site Components and Their Apparent Roles in Catalysis
Crystal Structures of Soybean .beta.-Amylase Reacted with .beta.-Maltose and Maltal: Active Site Components and Their Apparent Roles in Catalysis
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Crystal Structures of Soybean .beta.-Amylase Reacted with .beta.-Maltose and Maltal: Active Site Components and Their Apparent Roles in Catalysis

Mikami, Bunzo ; Degano, Massimo ; Hehre, Edward J ; Sacchettini, James C

Biochemistry (Easton), 1994-06, Vol.33 (25), p.7779-7787 [Periódico revisado por pares]

United States: American Chemical Society

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6
Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites
Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites
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Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites

Harris, David A ; Huber, Mary T ; Van Dijken, Peter ; Shyng, Show Ling ; Chait, Brian T ; Wang, Rong

Biochemistry (Easton), 1993-02, Vol.32 (4), p.1009-1016 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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7
The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants
The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants
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The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants

MacLeod, Alasdair M ; Lindhorst, Thisbe ; Withers, Stephen G ; Warren, R. Antony J

Biochemistry (Easton), 1994-05, Vol.33 (20), p.6371-6376 [Periódico revisado por pares]

United States: American Chemical Society

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8
Kinetic Mechanism of the Enantioselective Conversion of Styrene Oxide by Epoxide Hydrolase from Agrobacterium radiobacter AD1
Kinetic Mechanism of the Enantioselective Conversion of Styrene Oxide by Epoxide Hydrolase from Agrobacterium radiobacter AD1
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Kinetic Mechanism of the Enantioselective Conversion of Styrene Oxide by Epoxide Hydrolase from Agrobacterium radiobacter AD1

Rink, Rick ; Janssen, Dick B

Biochemistry (Easton), 1998-12, Vol.37 (51), p.18119-18127 [Periódico revisado por pares]

United States: American Chemical Society

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9
Mechanisms of Cellulases and Xylanases: A Detailed Kinetic Study of the Exo-.beta.-1,4-glycanase from Cellulomonas Fimi
Mechanisms of Cellulases and Xylanases: A Detailed Kinetic Study of the Exo-.beta.-1,4-glycanase from Cellulomonas Fimi
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Mechanisms of Cellulases and Xylanases: A Detailed Kinetic Study of the Exo-.beta.-1,4-glycanase from Cellulomonas Fimi

Tull, Dedreia ; Withers, Stephen G

Biochemistry (Easton), 1994-05, Vol.33 (20), p.6363-6370 [Periódico revisado por pares]

United States: American Chemical Society

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10
Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis
Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis
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Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis

Chen, Zhuo ; Jiang, James C ; Lin, Zhi Gong ; Lee, William R ; Baker, Michael E ; Chang, Simon H

Biochemistry (Easton), 1993-04, Vol.32 (13), p.3342-3346 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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