2XJ5
The structure of cytochrome c peroxidase Compound II
Summary for 2XJ5
| Entry DOI | 10.2210/pdb2xj5/pdb |
| Related | 1A2F 1A2G 1AA4 1AC4 1AC8 1AEB 1AED 1AEE 1AEF 1AEG 1AEH 1AEJ 1AEK 1AEM 1AEN 1AEO 1AEQ 1AES 1AET 1AEU 1AEV 1BEJ 1BEK 1BEM 1BEP 1BEQ 1BES 1BJ9 1BVA 1CCA 1CCB 1CCC 1CCE 1CCG 1CCI 1CCJ 1CCK 1CCL 1CCP 1CMP 1CMQ 1CMT 1CMU 1CPD 1CPE 1CPF 1CPG 1CYF 1DCC 1DJ1 1DJ5 1DS4 1DSE 1DSG 1DSO 1DSP 1EBE 1JCI 1JDR 1KOK 1KRJ 1KXM 1KXN 1MK8 1MKQ 1MKR 1ML2 1RYC 1S6V 1SDQ 1SOG 1STQ 1U74 1U75 1Z53 1ZBY 1ZBZ 2B0Z 2B10 2B11 2B12 2BCN 2CCP 2CEP 2CYP 2GB8 2PCB 2PCC 2V23 2V2E 2X07 2X08 2XIL 3CCP 3CCX 4CCP 4CCX 5CCP 6CCP 7CCP |
| Descriptor | CYTOCHROME C PEROXIDASE, MITOCHONDRIAL, PROTOPORPHYRIN IX CONTAINING FE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, ascorbate peroxidase, ferryl ion, ferrous heme |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Mitochondrion matrix: P00431 |
| Total number of polymer chains | 1 |
| Total formula weight | 35053.90 |
| Authors | Gumiero, A.,Raven, E.L.,Moody, P.C.E. (deposition date: 2010-07-02, release date: 2010-07-14, Last modification date: 2023-12-20) |
| Primary citation | Gumiero, A.,Metcalfe, C.L.,Pearson, A.R.,Raven, E.L.,Moody, P.C. Nature of the ferryl heme in compounds I and II. J. Biol. Chem., 286:1260-1268, 2011 Cited by PubMed Abstract: Heme enzymes are ubiquitous in biology and catalyze 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 a 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. PubMed: 21062738DOI: 10.1074/jbc.M110.183483 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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