The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.

Yachnin BJ, Lau PCK, Berghuis AM
Biochim Biophys Acta 1864(12):1641-1648 (2016 Dec)

PMID: 27570148 doi: 10.1016/j.bbapap.2016.08.015

Submitted to SASBDB: 2016 Aug 16 Published in SASBDB: 2016 Sep 1

SASDBA5 – Cyclohexanone monooxygenase, wild-type Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2 RgGuinier 2.7 nm Dmax 9.3 nm VolumePorod 110 nm3

SASDBB5 – Cyclohexanone monooxygenase, NADP+, wild-type Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Jan 27 RgGuinier 2.6 nm Dmax 8.0 nm VolumePorod 99 nm3

SASDBC5 – Cyclohexanone monooxygenase, NADP+ and cyclohexanone, wild-type Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+ 5 mM cyclohexanone, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2 RgGuinier 2.5 nm Dmax 7.8 nm VolumePorod 100 nm3

SASDBD5 – Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, wild-type Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+ 5 mM ε-caprolactone, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2 RgGuinier 2.5 nm Dmax 7.5 nm VolumePorod 99 nm3

SASDBE5 – Cyclohexanone monooxygenase, W492A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 25 RgGuinier 2.8 nm Dmax 9.5 nm VolumePorod 110 nm3

SASDBF5 – Cyclohexanone monooxygenase, NADP+, K501A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 2.6 nm Dmax 8.7 nm VolumePorod 100 nm3

SASDBG5 – Cyclohexanone monooxygenase, NADP+, W492A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+ 5 mM cyclohexanone, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 25 RgGuinier 2.6 nm Dmax 8.9 nm VolumePorod 96 nm3

SASDBH5 – Cyclohexanone monooxygenase, NADP+ and cyclohexanone, W492A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+ 5 mM cyclohexanone, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 25 RgGuinier 2.6 nm Dmax 8.9 nm VolumePorod 98 nm3

SASDBJ5 – Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, W492A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+ 5 mM ε-caprolactone, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 25 RgGuinier 2.6 nm Dmax 9.0 nm VolumePorod 100 nm3

SASDBK5 – Cyclohexanone monooxygenase, K328A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 2.8 nm Dmax 9.8 nm VolumePorod 110 nm3

SASDBL5 – Cyclohexanone monooxygenase, NADP+, K328A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 2.6 nm Dmax 8.4 nm VolumePorod 100 nm3

SASDBM5 – Cyclohexanone monooxygenase, K328A-W492A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Nov 17 RgGuinier 2.7 nm Dmax 9.4 nm VolumePorod 110 nm3

SASDBN5 – Cyclohexanone monooxygenase, NADP+, K328A-W492A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Nov 17 RgGuinier 2.6 nm Dmax 7.8 nm VolumePorod 96 nm3

SASDBP5 – Cyclohexanone monooxygenase, N497A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 2.9 nm Dmax 10.4 nm VolumePorod 120 nm3

SASDBQ5 – Cyclohexanone monooxygenase, NADP+, N497A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 2.7 nm Dmax 9.2 nm VolumePorod 100 nm3

SASDBR5 – Cyclohexanone monooxygenase, K501A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 3.0 nm Dmax 10.1 nm VolumePorod 120 nm3

SASDBS5 – Cyclohexanone monooxygenase, N497A-K501A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 3.0 nm Dmax 11.0 nm VolumePorod 130 nm3

SASDBT5 – Cyclohexanone monooxygenase, NADP+, N497A-K501A Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein Buffer: 50 mM Tris 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15 RgGuinier 2.8 nm Dmax 9.2 nm VolumePorod 110 nm3

SASDBU5 – Cyclopentadecanone monooxygenase, wild-type Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein Buffer: 50 mM Tris 2 mM TCEP, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Jan 27 RgGuinier 2.8 nm Dmax 10.4 nm VolumePorod 110 nm3

SASDBV5 – Cyclopentadecanone monooxygenase, NADP+, wild-type Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein Buffer: 50 mM Tris 2 mM TCEP 5 mM NADP+, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2 RgGuinier 2.7 nm Dmax 8.7 nm VolumePorod 120 nm3

SASDBW5 – Cyclopentadecanone monooxygenase, NADP+ and cyclopentadecanone, wild-type Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein Buffer: 50mM Tris 2mM TCEP 5mM NADP+ 1mM cyclopentadecanon, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2 RgGuinier 2.6 nm Dmax 9.0 nm VolumePorod 110 nm3

SASDBX5 – Cyclopentadecanone monooxygenase, NADP+ and ω-pentadecalactone, wild-type Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein Buffer: 50mM Tris mM TCEP 5mM NADP+ 1mM ω-pentadecalactone, pH: 8 Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2 RgGuinier 2.6 nm Dmax 9.0 nm VolumePorod 100 nm3