Catalase
From Proteopedia
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Catalase is a <scene name='46/467276/Cv/2'>tetramer of four polypeptide chains</scene>, each over 500 amino acids long. It contains <scene name='46/467276/Cv/3'>four porphyrin heme (iron) groups</scene> that allow the enzyme to react with the hydrogen peroxide. <scene name='46/467276/Cv/5'>Coordination of heme</scene> in ''E. coli'' catalase.<ref>PMID:11455600</ref> | Catalase is a <scene name='46/467276/Cv/2'>tetramer of four polypeptide chains</scene>, each over 500 amino acids long. It contains <scene name='46/467276/Cv/3'>four porphyrin heme (iron) groups</scene> that allow the enzyme to react with the hydrogen peroxide. <scene name='46/467276/Cv/5'>Coordination of heme</scene> in ''E. coli'' catalase.<ref>PMID:11455600</ref> | ||
| - | As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen. The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr357 in the fifth iron ligand, which can assist in the oxidation of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His74 and Asn147 with reaction intermediates. <br /> | + | As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen. The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr357 in the fifth iron ligand, which can assist in the oxidation of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His74 and Asn147 with reaction intermediates.<ref>PMID:21524057</ref> <br /> |
See more details in [[Ann Taylor/Catalase]] and [[Catalase 2CAG bcce2014]].<br /> | See more details in [[Ann Taylor/Catalase]] and [[Catalase 2CAG bcce2014]].<br /> | ||
See also [[Catalase (Hebrew)]]. | See also [[Catalase (Hebrew)]]. | ||
Revision as of 08:50, 23 November 2015
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3D Structures of catalase
Updated on 23-November-2015
References
- ↑ Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli. Proteins. 2001 Aug 15;44(3):270-81. PMID:11455600
- ↑ Purwar N, McGarry JM, Kostera J, Pacheco AA, Schmidt M. Interaction of Nitric Oxide with Catalase: Structural and Kinetic Analysis. Biochemistry. 2011 May 6. PMID:21524057 doi:10.1021/bi200130r
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Karsten Theis, Ann Taylor
