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Biochemistry
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June 4, 1996
Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3
I Sevrioukova, C Shaffer, D P Ballou, et al.
The Journal of Biological Chemistry
|
September 15, 1991
Catalytic function of tyrosine residues in para-hydroxybenzoate hydroxylase as determined by the study of site-directed mutants
B Entsch, B A Palfey, D P Ballou, et al.
The Journal of Biological Chemistry
|
December 10, 1983
Rapid reaction studies on the oxygenation reactions of catechol dioxygenase
T A Walsh, D P Ballou, R Mayer, et al.
Biochemistry
|
December 22, 1999
Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins
M Ortiz-Maldonado, D Gatti, D P Ballou, et al.
Biochemistry
|
February 15, 1994
Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp
B A Palfey, B Entsch, D P Ballou, et al.
The Journal of Biological Chemistry
|
January 5, 1987
Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum
J B Powlowski, S Dagley, V Massey, et al.
The Journal of Biological Chemistry
|
February 25, 1980
Oxygen reactivity of p-hydroxybenzoate hydroxylase containing 1-deaza-FAD
B Entsch, M Husain, D P Ballou, et al.
Biochemistry
|
July 16, 1996
Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys
G R Moran, B Entsch, B A Palfey, et al.
Biochemistry
|
July 27, 2001
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl-flavin
M Ortiz-Maldonado, S M Aeschliman, D P Ballou, et al.
Biochemistry
|
January 16, 1996
pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis
D L Gatti, B Entsch, D P Ballou, et al.
Page
of 11
Search research articles
Search
Showing results (51-60 of 102) with videos related to
Sort By:
Page
of 11
Biochemistry
|
June 4, 1996
Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3
I Sevrioukova, C Shaffer, D P Ballou, et al.
The Journal of Biological Chemistry
|
September 15, 1991
Catalytic function of tyrosine residues in para-hydroxybenzoate hydroxylase as determined by the study of site-directed mutants
B Entsch, B A Palfey, D P Ballou, et al.
The Journal of Biological Chemistry
|
December 10, 1983
Rapid reaction studies on the oxygenation reactions of catechol dioxygenase
T A Walsh, D P Ballou, R Mayer, et al.
Biochemistry
|
December 22, 1999
Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins
M Ortiz-Maldonado, D Gatti, D P Ballou, et al.
Biochemistry
|
February 15, 1994
Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp
B A Palfey, B Entsch, D P Ballou, et al.
The Journal of Biological Chemistry
|
January 5, 1987
Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum
J B Powlowski, S Dagley, V Massey, et al.
The Journal of Biological Chemistry
|
February 25, 1980
Oxygen reactivity of p-hydroxybenzoate hydroxylase containing 1-deaza-FAD
B Entsch, M Husain, D P Ballou, et al.
Biochemistry
|
July 16, 1996
Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys
G R Moran, B Entsch, B A Palfey, et al.
Biochemistry
|
July 27, 2001
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl-flavin
M Ortiz-Maldonado, S M Aeschliman, D P Ballou, et al.
Biochemistry
|
January 16, 1996
pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis
D L Gatti, B Entsch, D P Ballou, et al.
Page
of 11