Manganese peroxidase
From Proteopedia
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| - | + | <StructureSection load='3m5q' size='450' side='right' scene='' caption='Heme-containing glycosylated manganese peroxidase complex with glycerol, Mn+2 (purple) and Ca+2 (green) ions [[3m5q]]'> | |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
The Mn binding site of MnP contains the heme group which coordinates with the ion. The heme group is coordinated mostly by aromatic side chains<ref>PMID:20356630</ref>. | The Mn binding site of MnP contains the heme group which coordinates with the ion. The heme group is coordinated mostly by aromatic side chains<ref>PMID:20356630</ref>. | ||
| + | </StructureSection> | ||
==3D structures of manganese peroxidase== | ==3D structures of manganese peroxidase== | ||
Revision as of 08:44, 24 April 2016
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3D structures of manganese peroxidase
Updated on 24-April-2016
References
- ↑ Youngs HL, Sundaramoorthy M, Gold MH. Effects of cadmium on manganese peroxidase competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur J Biochem. 2000 Mar;267(6):1761-9. PMID:10712608
- ↑ Sundaramoorthy M, Gold MH, Poulos TL. Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J Inorg Biochem. 2010 Jun;104(6):683-90. Epub 2010 Mar 6. PMID:20356630 doi:10.1016/j.jinorgbio.2010.02.011
