Sandbox Reserved 1072: Difference between revisions

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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 H202 alternately oxidizes and reduces the heme iron at the active site. Within peroxidases, oxidation of heme iron involves a H202 molecules, similar to that in the catalase-catalyzed reaction. Reduction of the heme iron, however, involves hydrogen donors such as NADH, not a second H202 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 ~~struture~~ 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 H202 alternately oxidizes and reduces the heme iron at the active site. Within peroxidases, oxidation of heme iron involves a H202 molecules, similar to that in the catalase-catalyzed reaction. Reduction of the heme iron, however, involves hydrogen donors such as NADH, not a second H202 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==

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===Active Site===

[[Image:INH.png|300 px|left|thumb|'''Figure 2.''' Active Site with conserved amino acid residues.]]

[[Image:INH.png|300 px|left|thumb|'''Figure 2.''' Active Site with conserved amino acid residues. The green arrow represents the binding site.]]

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Sandbox Reserved 1072: Difference between revisions

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@@ Line 8: / Line 8: @@
 ===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 struture 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 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.
 ==Structure==
@@ Line 21: / Line 21: @@
 ===Active Site===
-[[Image:INH.png|300 px|left|thumb|'''Figure 2.''' Active Site with conserved amino acid residues.]]
+[[Image:INH.png|300 px|left|thumb|'''Figure 2.''' Active Site with conserved amino acid residues. The green arrow represents the binding site.]]
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