Stubbe J - Search Results

1

Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthase.

Jia Y, Kappock TJ, Frick T, Sinskey AJ, Stubbe J. Jia Y, et al. Among authors: stubbe j. Biochemistry. 2000 Apr 11;39(14):3927-36. doi: 10.1021/bi9928086. Biochemistry. 2000. PMID: 10747780

The model indicates that C130 is not involved in catalysis as previously proposed [Muh, U., Sinskey, A. J., Kirby, D. P., Lane, W. S., and Stubbe, J. (1999) Biochemistry 38, 826-837]. ...

The model indicates that C130 is not involved in catalysis as previously proposed [Muh, U., Sinskey, A. J., Kirby, D. P., Lane, W. S. …

2

A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing.

Mao SS, Holler TP, Yu GX, Bollinger JM Jr, Booker S, Johnston MI, Stubbe J. Mao SS, et al. Among authors: stubbe j. Biochemistry. 1992 Oct 13;31(40):9733-43. doi: 10.1021/bi00155a029. Biochemistry. 1992. PMID: 1382592

3

Interaction of C225SR1 mutant subunit of ribonucleotide reductase with R2 and nucleoside diphosphates: tales of a suicidal enzyme.

Mao SS, Holler TP, Bollinger JM Jr, Yu GX, Johnston MI, Stubbe J. Mao SS, et al. Among authors: stubbe j. Biochemistry. 1992 Oct 13;31(40):9744-51. doi: 10.1021/bi00155a030. Biochemistry. 1992. PMID: 1390750

4

Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity.

Mao SS, Yu GX, Chalfoun D, Stubbe J. Mao SS, et al. Among authors: stubbe j. Biochemistry. 1992 Oct 13;31(40):9752-9. doi: 10.1021/bi00155a031. Biochemistry. 1992. PMID: 1390751

5

Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.

Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM. Meyer E, et al. Among authors: stubbe j. Biochemistry. 1992 Jun 2;31(21):5022-32. doi: 10.1021/bi00136a016. Biochemistry. 1992. PMID: 1534690

6

Glycinamide ribonucleotide synthetase from Escherichia coli: cloning, overproduction, sequencing, isolation, and characterization.

Cheng YS, Shen Y, Rudolph J, Stern M, Stubbe J, Flannigan KA, Smith JM. Cheng YS, et al. Among authors: stubbe j. Biochemistry. 1990 Jan 9;29(1):218-27. doi: 10.1021/bi00453a030. Biochemistry. 1990. PMID: 2182115

7

Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization.

Schendel FJ, Mueller E, Stubbe J, Shiau A, Smith JM. Schendel FJ, et al. Among authors: stubbe j. Biochemistry. 1989 Mar 21;28(6):2459-71. doi: 10.1021/bi00432a017. Biochemistry. 1989. PMID: 2659070

8

Radicals in biological catalysis.

Stubbe J. Stubbe J. Biochemistry. 1988 May 31;27(11):3893-900. doi: 10.1021/bi00411a001. Biochemistry. 1988. PMID: 3046660 Review. No abstract available.

9

Sequence-specific double-strand cleavage of DNA by Fe-bleomycin. 1. The detection of sequence-specific double-strand breaks using hairpin oligonucleotides.

Absalon MJ, Kozarich JW, Stubbe J. Absalon MJ, et al. Among authors: stubbe j. Biochemistry. 1995 Feb 14;34(6):2065-75. doi: 10.1021/bi00006a029. Biochemistry. 1995. PMID: 7531498

10

Sequence-specific double-strand cleavage of DNA by Fe-bleomycin. 2. Mechanism and dynamics.

Absalon MJ, Wu W, Kozarich JW, Stubbe J. Absalon MJ, et al. Among authors: stubbe j. Biochemistry. 1995 Feb 14;34(6):2076-86. doi: 10.1021/bi00006a030. Biochemistry. 1995. PMID: 7531499

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