| Structural highlights
2xil is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , ,
| | Related: | 1cpg, 1bva, 2v23, 3ccx, 6ccp, 1aeu, 1dcc, 1s6v, 1bej, 1ml2, 1ccl, 1beq, 1aem, 1jci, 1u74, 2b10, 2pcc, 1aeb, 1cpd, 1ccg, 1cca, 1ac4, 1cmu, 1aeo, 1bep, 1aet, 2pcb, 1aeh, 1aev, 1kxn, 1aen, 1aeg, 4ccp, 5ccp, 2cep, 2x07, 1cmp, 1ryc, 1cce, 2b0z, 1bes, 1dsp, 1z53, 2b12, 1bem, 1mkr, 1sog, 1ccj, 1aee, 1a2f, 1cpe, 1jdr, 1dse, 1a2g, 1aes, 1bek, 1zbz, 1cck, 1mkq, 1mk8, 1ebe, 1cci, 1krj, 2b11, 1aef, 1cyf, 1aek, 1ccb, 1u75, 1ac8, 1dsg, 1dj1, 1dj5, 2ccp, 1cmt, 1aeq, 1aej, 1ds4, 7ccp, 1sdq, 2x08, 2gb8, 4ccx, 1kxm, 1kok, 1bj9, 2bcn, 1zby, 1ccp, 2cyp, 1dso, 1stq, 3ccp, 2v2e, 1aa4, 1aed, 1ccc, 1cmq, 1cpf |
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Heme enzymes are ubiquitous in biology and catalyse a vast array of biological redox processes. The formation of high-valent ferryl intermediates of the heme iron (known as Compounds I and Compound II) is implicated for number of catalytic heme enzymes, but these species are formed only transiently and thus have proved somewhat elusive. In consequence, there has been conflicting evidence as to the nature of these ferryl intermediates in a number of different heme enzymes, in particular the precise nature of the bond between the heme iron and the bound oxygen atom. In this work, we present high-resolution crystal structures of both Compound I and Compound II intermediates in two different heme peroxidase enzymes, cytochrome c peroxidase and ascorbate peroxidase, allowing direct and accurate comparison of the bonding interactions in the different intermediates. A consistent picture emerges across all structures, showing lengthening of the ferryl oxygen bond (and presumed protonation) on reduction of Compound I to Compound II. These data clarify long-standing inconsistencies on the nature of the ferryl heme species in these intermediates.
The nature of the ferryl heme in compounds I and II.,Gumiero A, Metcalfe CL, Pearson AR, Raven EL, Moody PC J Biol Chem. 2010 Nov 8. PMID:21062738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gumiero A, Metcalfe CL, Pearson AR, Raven EL, Moody PC. The nature of the ferryl heme in compounds I and II. J Biol Chem. 2010 Nov 8. PMID:21062738 doi:10.1074/jbc.M110.183483
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