{"id":1048,"date":"2017-10-27T16:46:28","date_gmt":"2017-10-27T16:46:28","guid":{"rendered":"https:\/\/courses.lumenlearning.com\/suny-nutrition\/?post_type=chapter&#038;p=1048"},"modified":"2017-11-14T17:54:06","modified_gmt":"2017-11-14T17:54:06","slug":"12-91-copper-functions","status":"publish","type":"chapter","link":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/chapter\/12-91-copper-functions\/","title":{"raw":"12.91 Copper Functions","rendered":"12.91 Copper Functions"},"content":{"raw":"<div class=\"__UNKNOWN__\">\r\n\r\nCopper has a number of functions that are described and shown below.\r\n\r\nTwo copper-containing proteins, ceruloplasmin and hephaestin, oxidize Fe2+ to Fe3+. Fe3+ is the form that binds to transferrin, as shown below<sup>1<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"939\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164429\/10000000000003AB0000021C44A7B1B0.png\" alt=\"\" width=\"939\" height=\"540\" \/> Figure 12.911 Transport and uptake of iron[\/caption]\r\n\r\n<\/div>\r\nBecause copper is needed for this function, it is important for iron absorption.\r\n\r\nCopper is also a cofactor for superoxide dismutase, which converts superoxide to hydrogen peroxide, as shown below.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"1139\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164432\/1000000000000473000002F5A403A9C6.png\" alt=\"\" width=\"1139\" height=\"757\" \/> Figure 12.912 Superoxide dismutase uses zinc as a cofactor[\/caption]\r\n\r\n<\/div>\r\nCopper is also needed for hormone synthesis. For example, it is a cofactor for dopamine beta-hydroxylase, which converts dopamine to norepinephrine, as shown below<sup>1<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"264\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164434\/1000020100000108000001467EB44654.png\" alt=\"\" width=\"264\" height=\"326\" \/> Figure 12.913 Dopamine beta-hydroxylase requires copper<sup>2<\/sup>[\/caption]\r\n\r\n<\/div>\r\nHopefully the following example looks vaguely familiar because we talked about this pathway in the the vitamin C functions subsection. Ascorbic acid reduces Cu2+ back to Cu1+ so that this enzyme can continue to function, as shown below<sup>1<\/sup>. This is analogous to how ascorbic acid reduces Fe3+ back to Fe2+ so proline and lysyl hydroxylases can continue to function.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"814\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164436\/100000000000032E0000024E50F24AA2.png\" alt=\"\" width=\"814\" height=\"590\" \/> Figure 12.914 Dopamine beta-hydroxylase[\/caption]\r\n\r\n<\/div>\r\nCytochrome c oxidase (complex IV) in the electron transport chain is a copper-containing enzyme that reduces oxygen to form water, as shown below<sup>1<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"953\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164438\/10000000000003B9000001D748EB40C8.png\" alt=\"\" width=\"953\" height=\"471\" \/> Figure 12.915 Cytochrome c oxidase (complex IV)[\/caption]\r\n\r\n<\/div>\r\nLysyl oxidase, an enzyme that is important for cross-linking between structural proteins (collagen and elastin), requires copper as a cofactor<sup>1<\/sup>.\r\n\r\n<b>References &amp; Links<\/b>\r\n\r\n1. Gropper SS, Smith JL, Groff JL. (2008) Advanced nutrition and human metabolism. Belmont, CA: Wadsworth Publishing.\r\n\r\n2. http:\/\/en.wikipedia.org\/wiki\/File:Catecholamines_biosynthesis.svg\r\n\r\n3. http:\/\/wikidoc.org\/index.php\/File:ETC.PNG\r\n\r\n<\/div>","rendered":"<div class=\"__UNKNOWN__\">\n<p>Copper has a number of functions that are described and shown below.<\/p>\n<p>Two copper-containing proteins, ceruloplasmin and hephaestin, oxidize Fe2+ to Fe3+. Fe3+ is the form that binds to transferrin, as shown below<sup>1<\/sup>.<\/p>\n<div>\n<div style=\"width: 949px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164429\/10000000000003AB0000021C44A7B1B0.png\" alt=\"\" width=\"939\" height=\"540\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.911 Transport and uptake of iron<\/p>\n<\/div>\n<\/div>\n<p>Because copper is needed for this function, it is important for iron absorption.<\/p>\n<p>Copper is also a cofactor for superoxide dismutase, which converts superoxide to hydrogen peroxide, as shown below.<\/p>\n<div>\n<div style=\"width: 1149px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164432\/1000000000000473000002F5A403A9C6.png\" alt=\"\" width=\"1139\" height=\"757\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.912 Superoxide dismutase uses zinc as a cofactor<\/p>\n<\/div>\n<\/div>\n<p>Copper is also needed for hormone synthesis. For example, it is a cofactor for dopamine beta-hydroxylase, which converts dopamine to norepinephrine, as shown below<sup>1<\/sup>.<\/p>\n<div>\n<div style=\"width: 274px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164434\/1000020100000108000001467EB44654.png\" alt=\"\" width=\"264\" height=\"326\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.913 Dopamine beta-hydroxylase requires copper<sup>2<\/sup><\/p>\n<\/div>\n<\/div>\n<p>Hopefully the following example looks vaguely familiar because we talked about this pathway in the the vitamin C functions subsection. Ascorbic acid reduces Cu2+ back to Cu1+ so that this enzyme can continue to function, as shown below<sup>1<\/sup>. This is analogous to how ascorbic acid reduces Fe3+ back to Fe2+ so proline and lysyl hydroxylases can continue to function.<\/p>\n<div>\n<div style=\"width: 824px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164436\/100000000000032E0000024E50F24AA2.png\" alt=\"\" width=\"814\" height=\"590\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.914 Dopamine beta-hydroxylase<\/p>\n<\/div>\n<\/div>\n<p>Cytochrome c oxidase (complex IV) in the electron transport chain is a copper-containing enzyme that reduces oxygen to form water, as shown below<sup>1<\/sup>.<\/p>\n<div>\n<div style=\"width: 963px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164438\/10000000000003B9000001D748EB40C8.png\" alt=\"\" width=\"953\" height=\"471\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.915 Cytochrome c oxidase (complex IV)<\/p>\n<\/div>\n<\/div>\n<p>Lysyl oxidase, an enzyme that is important for cross-linking between structural proteins (collagen and elastin), requires copper as a cofactor<sup>1<\/sup>.<\/p>\n<p><b>References &amp; Links<\/b><\/p>\n<p>1. Gropper SS, Smith JL, Groff JL. (2008) Advanced nutrition and human metabolism. Belmont, CA: Wadsworth Publishing.<\/p>\n<p>2. http:\/\/en.wikipedia.org\/wiki\/File:Catecholamines_biosynthesis.svg<\/p>\n<p>3. http:\/\/wikidoc.org\/index.php\/File:ETC.PNG<\/p>\n<\/div>\n\n\t\t\t <section class=\"citations-section\" role=\"contentinfo\">\n\t\t\t <h3>Candela Citations<\/h3>\n\t\t\t\t\t <div>\n\t\t\t\t\t\t <div id=\"citation-list-1048\">\n\t\t\t\t\t\t\t <div class=\"licensing\"><div class=\"license-attribution-dropdown-subheading\">CC licensed content, Shared previously<\/div><ul class=\"citation-list\"><li>Kansas State University Human Nutrition Flexbook. <strong>Authored by<\/strong>: Brian Lindshield. <strong>Provided by<\/strong>: Kansas State University. <strong>Located at<\/strong>: <a target=\"_blank\" href=\"http:\/\/goo.gl\/vOAnR\">http:\/\/goo.gl\/vOAnR<\/a>. <strong>License<\/strong>: <em><a target=\"_blank\" rel=\"license\" href=\"https:\/\/creativecommons.org\/licenses\/by\/4.0\/\">CC BY: Attribution<\/a><\/em><\/li><\/ul><\/div>\n\t\t\t\t\t\t <\/div>\n\t\t\t\t\t <\/div>\n\t\t\t <\/section>","protected":false},"author":311,"menu_order":35,"template":"","meta":{"_candela_citation":"[{\"type\":\"cc\",\"description\":\"Kansas State University Human Nutrition Flexbook\",\"author\":\"Brian Lindshield\",\"organization\":\"Kansas State University\",\"url\":\"goo.gl\/vOAnR\",\"project\":\"\",\"license\":\"cc-by\",\"license_terms\":\"\"}]","CANDELA_OUTCOMES_GUID":"","pb_show_title":"on","pb_short_title":"","pb_subtitle":"","pb_authors":[],"pb_section_license":""},"chapter-type":[],"contributor":[],"license":[],"class_list":["post-1048","chapter","type-chapter","status-publish","hentry"],"part":883,"_links":{"self":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1048","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters"}],"about":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/types\/chapter"}],"author":[{"embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/users\/311"}],"version-history":[{"count":4,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1048\/revisions"}],"predecessor-version":[{"id":1854,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1048\/revisions\/1854"}],"part":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/parts\/883"}],"metadata":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1048\/metadata\/"}],"wp:attachment":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/media?parent=1048"}],"wp:term":[{"taxonomy":"chapter-type","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapter-type?post=1048"},{"taxonomy":"contributor","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/contributor?post=1048"},{"taxonomy":"license","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/license?post=1048"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}