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Results 1 - 6 of 6
EC Number Metals/Ions Commentary Reference
Show all pathways known for 1.8.99.5Display the word mapDisplay the reaction diagram Show all sequences 1.8.99.5Cu the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory heme–copper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2 743347
Show all pathways known for 1.8.99.5Display the word mapDisplay the reaction diagram Show all sequences 1.8.99.5Fe the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A 743347
Show all pathways known for 1.8.99.5Display the word mapDisplay the reaction diagram Show all sequences 1.8.99.5Iron 20 mol of iron per mol of enzyme 733765
Show all pathways known for 1.8.99.5Display the word mapDisplay the reaction diagram Show all sequences 1.8.99.5Iron 20 to 21 nonheme iron atoms per enzyme molecule 394043
Show all pathways known for 1.8.99.5Display the word mapDisplay the reaction diagram Show all sequences 1.8.99.5Iron 24 mol of iron per mol of enzyme 394066
Show all pathways known for 1.8.99.5Display the word mapDisplay the reaction diagram Show all sequences 1.8.99.5Iron contains 22 non-heme iron atoms per molecule 734637
Results 1 - 6 of 6