Basran J - Search Results

1

Analysis of Reaction Intermediates in Tryptophan 2,3-Dioxygenase: A Comparison with Indoleamine 2,3-Dioxygenase.

Basran J, Booth ES, Lee M, Handa S, Raven EL. Basran J, et al. Biochemistry. 2016 Dec 13;55(49):6743-6750. doi: 10.1021/acs.biochem.6b01005. Epub 2016 Dec 1. Biochemistry. 2016. PMID: 27951658

2

Selective modification of alkylammonium ion specificity in trimethylamine dehydrogenase by the rational engineering of cation-pi bonding.

Basran J, Mewies M, Mathews FS, Scrutton NS. Basran J, et al. Biochemistry. 1997 Feb 25;36(8):1989-98. doi: 10.1021/bi962623o. Biochemistry. 1997. PMID: 9047296

3

Involvement of a flavin iminoquinone methide in the formation of 6-hydroxyflavin mononucleotide in trimethylamine dehydrogenase: a rationale for the existence of 8alpha-methyl and C6-linked covalent flavoproteins.

Mewies M, Basran J, Packman LC, Hille R, Scrutton NS. Mewies M, et al. Among authors: basran j. Biochemistry. 1997 Jun 10;36(23):7162-8. doi: 10.1021/bi970621d. Biochemistry. 1997. PMID: 9188716

4

Enzymatic H-transfer requires vibration-driven extreme tunneling.

Basran J, Sutcliffe MJ, Scrutton NS. Basran J, et al. Biochemistry. 1999 Mar 9;38(10):3218-22. doi: 10.1021/bi982719d. Biochemistry. 1999. PMID: 10074378

5

Redox cycles in trimethylamine dehydrogenase and mechanism of substrate inhibition.

Roberts P, Basran J, Wilson EK, Hille R, Scrutton NS. Roberts P, et al. Among authors: basran j. Biochemistry. 1999 Nov 9;38(45):14927-40. doi: 10.1021/bi9914098. Biochemistry. 1999. PMID: 10555975

6

Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry.

Basran J, Bhanji N, Basran A, Nietlispach D, Mistry S, Meskys R, Scrutton NS. Basran J, et al. Among authors: basran a. Biochemistry. 2002 Apr 9;41(14):4733-43. doi: 10.1021/bi025519h. Biochemistry. 2002. PMID: 11926836

7

Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants.

Lad L, Mewies M, Basran J, Scrutton NS, Raven EL. Lad L, et al. Among authors: basran j. Eur J Biochem. 2002 Jul;269(13):3182-92. doi: 10.1046/j.1432-1033.2002.02998.x. Eur J Biochem. 2002. PMID: 12084058 Free article.

8

Effects of multiple ligand binding on kinetic isotope effects in PQQ-dependent methanol dehydrogenase.

Hothi P, Basran J, Sutcliffe MJ, Scrutton NS. Hothi P, et al. Among authors: basran j. Biochemistry. 2003 Apr 8;42(13):3966-78. doi: 10.1021/bi027282v. Biochemistry. 2003. PMID: 12667088

9

Conformational mobility in the active site of a heme peroxidase.

Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL. Badyal SK, et al. Among authors: basran j. J Biol Chem. 2006 Aug 25;281(34):24512-20. doi: 10.1074/jbc.M602602200. Epub 2006 Jun 7. J Biol Chem. 2006. PMID: 16762924 Free article.

10

Mechanism of FAD reduction and role of active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylglycine oxidase: analysis of mutant structure and catalytic function.

Basran J, Fullerton S, Leys D, Scrutton NS. Basran J, et al. Biochemistry. 2006 Sep 19;45(37):11151-61. doi: 10.1021/bi061094d. Biochemistry. 2006. PMID: 16964976

Residues His-225 and Tyr-259 are located close to the FAD in the dehydrogenase active site of the bifunctional dimethylglycine oxidase (DMGO) of Arthrobacter globiformis. We have suggested [Leys, D., Basran, J., and Scrutton, N. S. (2003) EMBO J. 22, 4038-404 …

Residues His-225 and Tyr-259 are located close to the FAD in the dehydrogenase active site of the bifunctional dimethylglycine oxidase (DMGO …

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