Search results for: Denise A. Rock

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article

Kinetic Isotope Effects Implicate the Iron−Oxene as the Sole Oxidant in P450-Catalyzed N-Dealkylation

Tamara S. Dowers, Dan A. Rock, Denise A. Rock, Jeffrey P. Jones

Journal of the American Chemical Society > 2004 > 126 > 29 > 8868 - 8869

article

Quantitative Binding Models for CYP2C9 Based on Benzbromarone Analogues ^†

Charles W. Locuson, Denise A. Rock, Jeffrey P. Jones

Biochemistry > 2004 > 43 > 22 > 6948 - 6958

article

Evidence for Two Different Active Oxygen Species in Cytochrome P450 BM3 Mediated Sulfoxidation and N-Dealkylation Reactions

Trent J. Volz, Denise A. Rock, Jeffrey P. Jones

Journal of the American Chemical Society > 2002 > 124 > 33 > 9724 - 9725

article

Use of Kinetic Isotope Effects to Delineate the Role of Phenylalanine 87 in P450BM-3

Dan A Rock, Anthony E Boitano, Jan L Wahlstrom, Denise A Rock, more

Bioorganic Chemistry > 2002 > 30 > 2 > 107-118

The substrate oxidation rates of P450 _BM-3 are unparalleled in the cytochrome P450 (CYP) superfamily of enzymes. Furthermore, the bacterial enzyme, originating from Bacillus megaterium, has been used repeatedly as a model to study the metabolism of mammalian P450s. A specific example is presented where studying P450 _BM-3 substrate dynamics can define important enzyme-substrate characteristics,...

article

Active Site Mutations of Cytochrome P450cam Alter the Binding, Coupling, and Oxidation of the Foreign Substrates (R)- and (S)-2-Ethylhexanol

Kevin J. French, Dan A. Rock, Denise A. Rock, John I. Manchester, more

Archives of Biochemistry and Biophysics > 2002 > 398 > 2 > 188-197

Three factors are of primary importance with respect to designing efficient P450 biocatalysts. (1) The substrate must be oxidized at a significant rate. (2) The regioselectivity must heavily favor the desired product. (3) The enzyme must use the majority of the reducing equivalents from NADH or NADPH to produce product. The reaction we chose to study was oxidation of 2-ethylhexanol to 2-ethylhexanoic...

article

Benign Synthesis of 2-Ethylhexanoic Acid by Cytochrome P450cam: Enzymatic, Crystallographic, and Theoretical Studies ^†

Kevin J. French, Michael D. Strickler, Dan A. Rock, Denise A. Rock, more

Biochemistry > 2001 > 40 > 32 > 9532 - 9538

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Search results for: Denise A. Rock

Kinetic Isotope Effects Implicate the Iron−Oxene as the Sole Oxidant in P450-Catalyzed N-Dealkylation

Quantitative Binding Models for CYP2C9 Based on Benzbromarone Analogues †

Evidence for Two Different Active Oxygen Species in Cytochrome P450 BM3 Mediated Sulfoxidation and N-Dealkylation Reactions

Use of Kinetic Isotope Effects to Delineate the Role of Phenylalanine 87 in P450BM-3

Active Site Mutations of Cytochrome P450cam Alter the Binding, Coupling, and Oxidation of the Foreign Substrates (R)- and (S)-2-Ethylhexanol

Benign Synthesis of 2-Ethylhexanoic Acid by Cytochrome P450cam: Enzymatic, Crystallographic, and Theoretical Studies †

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Quantitative Binding Models for CYP2C9 Based on Benzbromarone Analogues ^†

Benign Synthesis of 2-Ethylhexanoic Acid by Cytochrome P450cam: Enzymatic, Crystallographic, and Theoretical Studies ^†