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Unformatted text preview: DOI: 10.1126/science.1198858 , 1633 (2010); 330 Science , et al. Costas M. Soukoulis More Bulky and Less Lossy-- Optical Metamaterials This copy is for your personal, non-commercial use only. clicking here. colleagues, clients, or customers by , you can order high-quality copies for your If you wish to distribute this article to others here. following the guidelines can be obtained by Permission to republish or repurpose articles or portions of articles ): March 1, 2011 www.sciencemag.org (this infomation is current as of The following resources related to this article are available online at http://www.sciencemag.org/content/330/6011/1633.full.html version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/content/330/6011/1633.full.html#ref-list-1 , 2 of which can be accessed free: cites 14 articles This article http://www.sciencemag.org/cgi/collection/mat_sci Materials Science subject collections: This article appears in the following registered trademark of AAAS. is a Science 2010 by the American Association for the Advancement of Science; all rights reserved. The title Copyright American Association for the Advancement of Science, 1200 New York Avenue NW, Washington, DC 20005. (print ISSN 0036-8075; online ISSN 1095-9203) is published weekly, except the last week in December, by the Science on March 1, 2011 www.sciencemag.org Downloaded from www.sciencemag.org SCIENCE VOL 330 17 DECEMBER 2010 1633 PERSPECTIVES Advanced techniques for bulk fabrication and loss reduction provide good prospects for practical optical metamaterials. oxidase from Pseudomonas stutzeri ( 11 ) is also informative. Although the cbb 3 enzyme appears to be closer to cNOR than does ba 3 , similarities in the amino acid sequences of NorB and subunit I of cbb 3 are low (<40%). Regardless, the two proteins exhibit highly similar three-dimensional structures. Spe- cifically, 12 central transmembrane heli- ces are conserved that share a topology of tightly packed helices arranged around a low- spin heme and a binuclear active site (i.e., a heme b 3 /Fe B or a heme a 3 /Cu B ). In ba 3 , the active-site heme a 3 /Cu B center is buried in the hydrophobic core of the enzyme, requir- ing that both polar (H + , e , and H 2 O) and lipo- philic (O 2 ) reactants move along structurally specifi ed pathways to their intended destina- tions. In cNOR, the active-site heme b 3 /Fe B is found essentially at the same location in the hydrophobic core. The three histidine side chains that coordinate the Cu B in HCO are conserved in cNOR and are supplemented with a glutamyl carboxylate group, providing a favorable coordination shell for an iron ion at the Fe B site....
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