InChI=1S/C34H36N4O6.Fe/c1- 7- 20- 17(3) 23- 13- 24- 19(5) 22(9- 10- 31(39) 40) 28(37- 24) 16- 30- 34(44,12- 11- 32(41) 42) 33(6,43) 29(38- 30) 15- 27- 21(8- 2) 18(4) 25(36- 27) 14- 26(20) 35- 23;/h7- 8,13- 16,43- 44H,1- 2,9- 12H2,3- 6H3,(H4,35,36,37,38,39,40,41,42) ;/q;+2/p- 4/t33- ,34+;/m0./s1 |
GFRHEDKPMCXPFU-XCVPDAMTSA-J |
Cc1c(C=C) c2C=C3[N+] 4=C(C=c5c(CCC([O- ] ) =O) c(C) c6=CC7=[N+] 8C(=Cc1n2[Fe- - ] 48n56) C(C=C) =C7C) [C@] (O) (CCC([O- ] ) =O) [C@@] 3(C) O |
|
cofactor
An organic molecule or ion (usually a metal ion) that is required by an enzyme for its activity. It may be attached either loosely (coenzyme) or tightly (prosthetic group).
|
|
View more via ChEBI Ontology
{3,3'- [(2RS,3SR)- 7,12- diethenyl- 2,3- dihydroxy- 3,8,13,17- tetramethyl- 2,3- dihydroporphyrin- 2,18- diyl- κ4N21,N22,N23,N24]dipropanoato(4−)}ferrate(2)
|
ferroheme d cis-diol(2−)
|
ChEBI
|
ferroheme d(2−)
|
ChEBI
|
haem d cis-diol(2−)
|
ChEBI
|
heme d cis-diol
|
UniProt
|
heme d(2−)
|
ChEBI
|
Murshudov GN, Grebenko AI, Barynin V, Dauter Z, Wilson KS, Vainshtein BK, Melik-Adamyan W, Bravo J, Ferrán JM, Ferrer JC, Switala J, Loewen PC, Fita I (1996) Structure of the heme d of Penicillium vitale and Escherichia coli catalases. The Journal of biological chemistry 271, 8863-8868 [PubMed:8621527] [show Abstract] A heme d prosthetic group with the configuration of a cis-hydroxychlorin gamma-spirolactone has been found in the crystal structures of Penicillium vitale catalase and Escherichia coli catalase hydroperoxidase II (HPII). The absolute stereochemistry of the two heme d chiral carbon atoms has been shown to be identical. For both catalases the heme d is rotated 180 degrees about the axis defined by the alpha-gamma-meso carbon atoms, with respect to the orientation found for heme b in beef liver catalase. Only six residues in the heme pocket, preserved in P. vitale and HPII, differ from those found in the bovine catalase. In the crystal structure of the inactive N201H variant of HPII catalase the prosthetic group remains as heme b, although its orientation is the same as in the wild type enzyme. These structural results confirm the observation that heme d is formed from protoheme in the interior of the catalase molecule through a self-catalyzed reaction. | Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I (1995) Crystal structure of catalase HPII from Escherichia coli. Structure (London, England : 1993) 3, 491-502 [PubMed:7663946] [show Abstract]
BackgroundCatalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. It serves, in part, to protect the cell from the toxic effects of small peroxides. Escherichia coli produces two catalases, HPI and HPII, that are quite distinct from other catalases in physical structure and catalytic properties. HPII, studied in this work, is encoded by the katE gene, and has been characterized as an oligomeric, monofunctional catalase containing one cis-heme d prosthetic group per subunit of 753 residues.ResultsThe crystal structure of catalase HPII from E. coli has been determined to 2.8 A resolution. The asymmetric unit of the crystal contains a whole molecule, which is a tetramer with accurate 222 point group symmetry. In the model built, that includes residues 27-753 and one heme group per monomer, strict non-crystallographic symmetry has been maintained. The crystallographic agreement R-factor is 20.1% for 58,477 reflections in the resolution shell 8.0-2.8 A.ConclusionsDespite differences in size and chemical properties, which were suggestive of a unique catalase, the deduced structure of HPII is related to the structure of catalase from Penicillium vitale, whose sequence is not yet known. In particular, both molecules have an additional C-terminal domain that is absent in the bovine catalase. This extra domain contains a Rossmann fold but no bound nucleotides have been detected, and its physiological role is unknown. In HPII, the heme group is modified to a heme d and inverted with respect to the orientation determined in all previously reported heme catalases. HPII is the largest catalase for which the structure has been determined to almost atomic resolution. |
|