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S C Tu

Showing results (41-50 of 69) with videos related to

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Archives of Biochemistry and Biophysics|March 1, 1979
Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductaseS C Tu, J E Becvar, J W Hastings
Biochemistry|May 2, 1978
Activity and stability of the luciferase--flavin intermediateJ E Becvar, S C Tu, J W Hastings
Biochemistry|February 24, 1987
Pseudomonas cepacia 3-hydroxybenzoate 6-hydroxylase: stereochemistry, isotope effects, and kinetic mechanismY M Yu, L H Wang, S C Tu
Photochemistry and Photobiology|July 27, 1999
Computational analysis of the oxygen addition at the C4a site of reduced flavin in the bacterial luciferase bioluminescence reactionN Wada, T Sugimoto, H Watanabe, et al.
Journal of Bacteriology|June 1, 1994
Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzymeB Lei, M Liu, S Huang, et al.
Biochemistry|March 21, 1978
Structural studies on bacterial luciferase using energy transfer and emission anisotropyS C Tu, C W Wu, J W Hastings
The Journal of Biological Chemistry|January 25, 1984
Apoenzyme of Pseudomonas cepacia salicylate hydroxylase. Preparation, fluorescence property, and nature of flavin bindingL H Wang, S C Tu, R C Lusk
Biochemistry|May 6, 1975
Photoexcited bacterial bioluminescence. Identity and properties of the photoexcitable luciferaseS C Tu, C A Waters, J W Hastings
Biochemistry|May 3, 1988
Studies of electron-transfer properties of salicylate hydroxylase from Pseudomonas cepacia and effects of salicylate and benzoate bindingG H Einarsdottir, M T Stankovich, S C Tu
Biochemistry|October 22, 1996
Flavin reductase P: structure of a dimeric enzyme that reduces flavinJ J Tanner, B Lei, S C Tu, et al.
Pageof 7

Showing results (41-50 of 69) with videos related to

Sort By:
Pageof 7
Archives of Biochemistry and Biophysics|March 1, 1979
Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductaseS C Tu, J E Becvar, J W Hastings
Biochemistry|May 2, 1978
Activity and stability of the luciferase--flavin intermediateJ E Becvar, S C Tu, J W Hastings
Biochemistry|February 24, 1987
Pseudomonas cepacia 3-hydroxybenzoate 6-hydroxylase: stereochemistry, isotope effects, and kinetic mechanismY M Yu, L H Wang, S C Tu
Photochemistry and Photobiology|July 27, 1999
Computational analysis of the oxygen addition at the C4a site of reduced flavin in the bacterial luciferase bioluminescence reactionN Wada, T Sugimoto, H Watanabe, et al.
Journal of Bacteriology|June 1, 1994
Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzymeB Lei, M Liu, S Huang, et al.
Biochemistry|March 21, 1978
Structural studies on bacterial luciferase using energy transfer and emission anisotropyS C Tu, C W Wu, J W Hastings
The Journal of Biological Chemistry|January 25, 1984
Apoenzyme of Pseudomonas cepacia salicylate hydroxylase. Preparation, fluorescence property, and nature of flavin bindingL H Wang, S C Tu, R C Lusk
Biochemistry|May 6, 1975
Photoexcited bacterial bioluminescence. Identity and properties of the photoexcitable luciferaseS C Tu, C A Waters, J W Hastings
Biochemistry|May 3, 1988
Studies of electron-transfer properties of salicylate hydroxylase from Pseudomonas cepacia and effects of salicylate and benzoate bindingG H Einarsdottir, M T Stankovich, S C Tu
Biochemistry|October 22, 1996
Flavin reductase P: structure of a dimeric enzyme that reduces flavinJ J Tanner, B Lei, S C Tu, et al.
Pageof 7