{"id":1026,"date":"2017-10-27T16:42:44","date_gmt":"2017-10-27T16:42:44","guid":{"rendered":"https:\/\/courses.lumenlearning.com\/suny-nutrition\/?post_type=chapter&#038;p=1026"},"modified":"2017-11-14T17:44:33","modified_gmt":"2017-11-14T17:44:33","slug":"12-73-iron-functions","status":"publish","type":"chapter","link":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/chapter\/12-73-iron-functions\/","title":{"raw":"12.73 Iron Functions","rendered":"12.73 Iron Functions"},"content":{"raw":"<div class=\"__UNKNOWN__\">\r\n\r\nAs we talked about in the previous subsection, there are 3 primary functional iron subcompartments.\r\n\r\n1. Hemoglobin\r\n\r\n2. Myoglobin\r\n\r\n3. Iron-containing enzymes\r\n\r\nHemoglobin contains heme that is responsible for red blood cells\u2019 red color. Hemoglobin carries oxygen to tissues. The function of hemoglobin can be seen in the link below.\r\n<table><colgroup> <col \/><\/colgroup>\r\n<tbody>\r\n<tr>\r\n<td><b>Web Link<\/b>\r\n\r\n-<u>Hemoglobin<\/u><\/td>\r\n<\/tr>\r\n<\/tbody>\r\n<\/table>\r\nMyoglobin is similar to hemoglobin in that it can bind oxygen. However, instead of being found in blood, it is found in muscle. The color of meat products is a result of the state that myoglobin is in, as shown in the link below.\r\n<table><colgroup> <col \/><\/colgroup>\r\n<tbody>\r\n<tr>\r\n<td><b>Web Link<\/b>\r\n\r\n-<u>Myoglobin &amp; Meat Color<\/u><\/td>\r\n<\/tr>\r\n<\/tbody>\r\n<\/table>\r\nThere are a number of enzymes that use iron as a cofactor. We've already talked about two in this class.\r\n\r\nIron is a cofactor for the antioxidant enzyme, catalase, that converts hydrogen peroxide to water, 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\/27164057\/1000000000000473000002F5A403A9C6.png\" alt=\"\" width=\"1139\" height=\"757\" \/> Figure 12.731 Catalase uses iron as a cofactor[\/caption]\r\n\r\n<\/div>\r\nIron is also a cofactor for proline and lysyl hydroxylases that are important in collagen cross-linking. This will be discussed further in the vitamin C section. The function of these enzymes is shown below.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"865\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164100\/10000000000003610000024F1C01559B.png\" alt=\"\" width=\"865\" height=\"591\" \/> Figure 12.732 Importance of ascorbic acid and iron to proline and lysyl hydroxylases.[\/caption]\r\n\r\n<\/div>\r\nHeme iron is also found in cytochromes, like cytochrome c in the electron transport chain as shown below<sup>1<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"945\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164102\/10000000000003B1000001D303C4F24B.png\" alt=\"\" width=\"945\" height=\"467\" \/> Figure 12.733 Cytochrome c in the electron transport chain contains\u00a0<span style=\"font-size: 16px\">iron<\/span><sup>2<\/sup>[\/caption]\r\n\r\n<\/div>\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:\/\/wikidoc.org\/index.php\/File:ETC.PNG\r\n\r\n<b>Links<\/b>\r\n\r\nHemoglobin - http:\/\/www.nlm.nih.gov\/medlineplus\/ency\/imagepages\/19510.htm\r\n\r\nMyoglobin &amp; Meat Color - http:\/\/meatisneat.files.wordpress.com\/2009\/09\/slide11.jpg\r\n\r\n<\/div>","rendered":"<div class=\"__UNKNOWN__\">\n<p>As we talked about in the previous subsection, there are 3 primary functional iron subcompartments.<\/p>\n<p>1. Hemoglobin<\/p>\n<p>2. Myoglobin<\/p>\n<p>3. Iron-containing enzymes<\/p>\n<p>Hemoglobin contains heme that is responsible for red blood cells\u2019 red color. Hemoglobin carries oxygen to tissues. The function of hemoglobin can be seen in the link below.<\/p>\n<table>\n<colgroup>\n<col \/><\/colgroup>\n<tbody>\n<tr>\n<td><b>Web Link<\/b><\/p>\n<p>&#8211;<u>Hemoglobin<\/u><\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>Myoglobin is similar to hemoglobin in that it can bind oxygen. However, instead of being found in blood, it is found in muscle. The color of meat products is a result of the state that myoglobin is in, as shown in the link below.<\/p>\n<table>\n<colgroup>\n<col \/><\/colgroup>\n<tbody>\n<tr>\n<td><b>Web Link<\/b><\/p>\n<p>&#8211;<u>Myoglobin &amp; Meat Color<\/u><\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>There are a number of enzymes that use iron as a cofactor. We&#8217;ve already talked about two in this class.<\/p>\n<p>Iron is a cofactor for the antioxidant enzyme, catalase, that converts hydrogen peroxide to water, 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\/27164057\/1000000000000473000002F5A403A9C6.png\" alt=\"\" width=\"1139\" height=\"757\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.731 Catalase uses iron as a cofactor<\/p>\n<\/div>\n<\/div>\n<p>Iron is also a cofactor for proline and lysyl hydroxylases that are important in collagen cross-linking. This will be discussed further in the vitamin C section. The function of these enzymes is shown below.<\/p>\n<div>\n<div style=\"width: 875px\" 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\/27164100\/10000000000003610000024F1C01559B.png\" alt=\"\" width=\"865\" height=\"591\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.732 Importance of ascorbic acid and iron to proline and lysyl hydroxylases.<\/p>\n<\/div>\n<\/div>\n<p>Heme iron is also found in cytochromes, like cytochrome c in the electron transport chain as shown below<sup>1<\/sup>.<\/p>\n<div>\n<div style=\"width: 955px\" 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\/27164102\/10000000000003B1000001D303C4F24B.png\" alt=\"\" width=\"945\" height=\"467\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.733 Cytochrome c in the electron transport chain contains\u00a0<span style=\"font-size: 16px\">iron<\/span><sup>2<\/sup><\/p>\n<\/div>\n<\/div>\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:\/\/wikidoc.org\/index.php\/File:ETC.PNG<\/p>\n<p><b>Links<\/b><\/p>\n<p>Hemoglobin &#8211; http:\/\/www.nlm.nih.gov\/medlineplus\/ency\/imagepages\/19510.htm<\/p>\n<p>Myoglobin &amp; Meat Color &#8211; http:\/\/meatisneat.files.wordpress.com\/2009\/09\/slide11.jpg<\/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-1026\">\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":5759,"menu_order":29,"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-1026","chapter","type-chapter","status-publish","hentry"],"part":883,"_links":{"self":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1026","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters"}],"about":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/types\/chapter"}],"author":[{"embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/users\/5759"}],"version-history":[{"count":4,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1026\/revisions"}],"predecessor-version":[{"id":1847,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1026\/revisions\/1847"}],"part":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/parts\/883"}],"metadata":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1026\/metadata\/"}],"wp:attachment":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/media?parent=1026"}],"wp:term":[{"taxonomy":"chapter-type","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapter-type?post=1026"},{"taxonomy":"contributor","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/contributor?post=1026"},{"taxonomy":"license","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/license?post=1026"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}