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- Σπυριδων Ζαΐμης
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1 Supporting Information Kβ Valence to Core X-ray Emission Studies of Cu(I) binding proteins with mixed Methionine Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase. Vlad Martin-Diaconescu, Kelly N. Chacón, Mario Delgado, Dimosthenis Sokaras, Tsu-Chien Weng, Serena DeBeer $* and Ninian J. Blackburn * Max Planck Institute for Chemical Energy Conversion, Stiftstr , D Mülheim an der Ruhr, Mülheim an der Ruhr, Germany Institute of Environmental Health, Oregon Health & Sciences University, Mail Code HRC3, 3181 SW Sam Jackson Park Road, Portland, OR Stanford Synchrotron Radiation Lightsource, 2575 Sand Hill Road, Menlo Park, CA 9725 $ Cornell University, Department of Chemistry and Chemical Biology, Ithaca, New York, 14853, United States (Current affiliation) Group de Química Bioinorgànica, Supramolecular i Catàlisi (QBIS-CAT), Institut de Química Computacional i Catàlisi (IQCC), Departament de Química, Universitat de Girona, Campus Montilivi, 1771 Girona (Spain) (Current affiliation) Reed College - Department of Chemistry, 323 SE Woodstock Blvd., Portland OR 9722 (Current affiliation) Inorganic Chemistry and Catalysis Group, Debye Institute for Nanomaterials Science, Utrecht University, 3584 CG, Utrecht, the Netherlands (Current affiliation) Center for High Pressure Science & Technology Advanced Research #6-48, 169 Cailun Rd., Pudong, Shanghai 2123, P. R. China * Corresponding Authors serena.debeer@cec.mpg.de; blackbni@ohsu.edu Tel.: ; Fax: Received: Running Title: XES of His-Met-containing Copper Proteins S1
2 Table of Contents Section S1 - Representative fits of the Experimental XES Spectra S3 Section S2 - XYZ of geometry optimized protein metal site S6 Section S3 - XYZ of Truncated Models S11 Section S4 - XYZ of CusB Geometry Study S13 Section S5 - XYZ of PHM CuH Geometry Study S14 Section S6 - Overlays of calculated VtC XES from truncated and full models S15 Section S7 - Overlays of additionally calculated VtC XES for CusF S15 S2
3 Section S1 - Representative fits of the Experimental XES Spectra 45 a) 1.5 b) 4 35 Experimental data Average of good fits Fig. S1.1- Average of good fits a) in the Kβ mainline region; and b) in the VtC region for CusF. Colored features in b) correspond to peak features in the VtC region contributing to the total area. In gray dotted lines are shown, the offset, the tails from the Kβ mainline peak features (shown in a), and the two features above 898 ev corresponding to K+L excitations a) Experimental data Average of good fits 4 x 1 3 b) Fig. S1.2- Average of good fits a) in the Kβ mainline region; and b) in the VtC region for CusB. Colored features in b) correspond to peak features in the VtC region contributing to the total area. In gray dotted lines are shown, the offset, the tails from the Kβ mainline peak features (shown in a), and the two features above 898 ev corresponding to K+L excitations. S3
4 .14 a) 5 x 1 3 b).12.1 Experimental data Average of good fits Fig. S1.3- Average of good fits a) in the Kβ mainline region; and b) in the VtC region for PHMCu M. Colored features in b) correspond to peak features in the VtC region contributing to the total area. In gray dotted lines are shown, the offset, the tails from the Kβ mainline peak features (shown in a), and the two features above 898 ev corresponding to K+L excitations a) Experimental data Average of good fits 5 x b) Fig. S1.4- Average of good fits a) in the Kβ mainline region; and b) in the VtC region for PHM- CO. Colored features in b) correspond to peak features in the VtC region contributing to the total area. In gray dotted lines are shown, the offset, the tails from the Kβ mainline peak features (shown in a), and the two features above 898 ev corresponding to K+L excitations. S4
5 a) Experimental data Average of good fits 3 x 1 3 b) Fig. S1.5- Average of good fits a) in the Kβ mainline region; and b) in the VtC region for PHMCu H. Colored features in b) correspond to peak features in the VtC region contributing to the total area. In gray dotted lines are shown, the offset, the tails from the Kβ mainline peak features (shown in a), and the two features above 898 ev corresponding to K+L excitations. Fig. S1.6- Normalized VtC XES reflecting the results from the fits for CuB and CusF Fig. S1.7- Normalized VtC XES reflecting the results from the fits for PHMCu H, PHM-CO and PHMCu M. S5
6 Section S2 - XYZ of geometry optimized protein metal site: CusB (CuMet 3), CusF (CuMet 2His 1), PHM Cu M site (CuMet 1His 2), and PHM CuH site (CuHis 3). CusB-CuMet3 Cu N C C O C C S C H H H H H H H H H H O H N C C O C C S C H H H H H H H H H H O H N C C O C C S C H H H H H H H H H H O H S6
7 CusF-CuMet 2His 1 N C C O C C C N C N N C C O C C C C C C N C C C N C C O C C S C N C C O C C O N C C O C C S C Cu C H H H H H H H H H H H H H H H H H H H H H H H H H H H H H H S7
8 H H H H H H H H H H H H H H H H H H H H PHMCu M-CuMet 1His 2 N C C O C C C N C N N C C O C C O N C C O C C C N C N N C C O C C S C Cu H H H H H H H H H H H H H H H H H H H H H S8
9 H H H H H H H H H H H H H PHMCu H-CuHis 3 N C C O C C N C C N N C C O C C N C C N C C C N C C N Cu H H H H H H H H H H H H H H H H H H H H H H H H S9
10 PHMCu MCO-CuMet 1His 2CO N C C O C C C N C N N C C O C C O N C C O C C C N C N N C C O C C S C Cu H H H H H H H H H H H H H H H H H H H H H H H H H H H H H H H H H H C O S1
11 Section S3 - XYZ of truncated metal site models: CusB (CuS 3), CusF (CuS 2I 1), PHM Cu M site (CuS 1I 2), PHM Cu H site (CuI 3) and PHM Cu M-CO (CuS 1I 2CO). Where S = S(CH 3) 2; I = imidazole. CuS3 Cu C S C H H H H H C S C H H H H H C S C H H H H H H H H CuS2I1 H C C N C N H C C C C C N C C C H C S C C S C Cu H H H H H H H H H H H H H H H H H H H H CuS 1I 2 H C C N C N H C C N C N H C S C Cu H H H H H H H H H H H CuI 3 H C N C C N H C N C S11
12 C N H C N C C N Cu H H H H H H H H H CuS1I2CO H C C N C N H C C N C N H C S C Cu H H H H H H H H H H H C O S12
13 Section S4 - XYZ of truncated metal site models for CusF (CuI 1S 2; where I = imidazole; S= S(CH 3) 2) with S-Cu-S bond angles at 75 o and 95 o. 116 o Cu C N C H N C H H C S C H H H H H C S C H H H H H H H o Cu C N C H N C H H C S C H H H H H C S C H H H H H H H H o Cu C N C H N C H H C S C H H H H H C S C H H H H H H H H S13
14 Section S5 - XYZ of truncated metal site models for PHM Cu H (CuI 3; where I - imidazole) with different coordination geometries. T-Shaped Cu N C C N C N C C N C N C C N C H H H H H H H H H H H H Trigonal pyramidal Cu N C C N C N C C N C H H H H H H H H H C C H C H N N H Trigonal planar Cu N C C N C N C C N C N C C N C H H H H H H H H H H H H S14
15 Section S6 - Overlays of calculated VtC XES from truncated and full models Section S7 - Overlays of additionally calculated VtC XES for CusF (S 2I 1; where S = S(CH 3) 2, I = imidazole). (1) The imidazole - Cu bond was set to 2.1 Å ( +.1 Å; longer Cu-N bond); (2) The imidazole -Cu bond was set to 1.87 Å (-.1 Å; shorter Cu-N bond) resulting in Cu-S bonds at 2.35 Å and 2.32 Å (+.7 Å; longer Cu-S bonds); (3) the Cu center was moved out of plane of to yield a C 3v pyramidal geometry. 116 o D3h model of CusF with S-Cu-S angle of 116 o lacking tryptophan residue (section S4); CusF truncated CusF model (with tryptophan residue). S15
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Cite as: Pol Antras, course materials for International Economics I, Spring MIT OpenCourseWare (http://ocw.mit.edu/), Massachusetts
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