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OCA, Elizabeth Hughes, Nicole Zimmerman, Geoffrey C. Hoops, David Emch, Isobel Bowles, Jack Trittipo

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 ===Catalase Peroxidases===
-Catalase-peroxidases are enzymes that degrade hydrogen peroxide. Catalase converts two equivalents of hydrogen peroxide into water and oxygen via a two-step reaction  cycle in which H<sub>2</sub>0<sub>2</sub> alternately oxidizes and reduces the heme iron at the active site. Within peroxidases, oxidation of heme iron involves a H<sub>2</sub>0<sub>2</sub> molecules, similar to that in the catalase-catalyzed reaction. Reduction of the heme iron, however, involves hydrogen donors such as NADH, not a second H<sub>2</sub>0<sub>2</sub> molcule <ref name="three">PMID: 12172540</ref>. Catalase-Peroxidases that have been characterized are either homodimers or homotetramers and contain a single heme ''b'' cofactor at the active site. Usually, the primary structure of the subunit can be divided into two halves that have a high level of sequence similarity, most likely due to a gene duplication event.
+Catalase-peroxidases are enzymes that degrade hydrogen peroxide. Catalase converts two equivalents of hydrogen peroxide into water and oxygen via a two-step reaction  cycle in which H<sub>2</sub>0<sub>2</sub> alternately oxidizes and reduces the heme iron at the active site. Within peroxidases, oxidation of heme iron involves H<sub>2</sub>0<sub>2</sub> molecules, similar to that in the catalase-catalyzed reaction. Reduction of the heme iron, however, involves hydrogen donors such as NADH, not a second H<sub>2</sub>0<sub>2</sub> molcule <ref name="three">PMID: 12172540</ref>. Catalase-Peroxidases that have been characterized are either homodimers or homotetramers and contain a single heme ''b'' cofactor at the active site. Usually, the primary structure of the subunit can be divided into two halves that have a high level of sequence similarity, most likely due to a gene duplication event.
 ==Structure==