1976
DOI: 10.1021/ja00425a008
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Axial ligation modes in iron(III) porphyrins. Models for the oxidized reaction states of cytochrome P-450 enzymes and the molecular structure of iron(III) protoporphyrin IX dimethyl ester p-nitrobenzenethiolate

Abstract: Bond Average Type Bond Average TypeC(30)-O(2)-Me(l) 117.2 (8) C(7)-C(8)-C(25)-C(26) -16 (2) C(33)-0(3)-Me(2) 116.1 (7) C(9)-C(8)-C(25)-C(26) 166 (1) C(36)-C(35)-C(40) 118.1 (6) 120.0 (24) C-C-Cphenyi C(13)-C(28)-C(29)-C(30) 76 (1) C(35)-C(36)-C(37) 122.3 (7) C(28)-C(29)-C(30)-O(l) 37 (1) C(36)-C(37)-C(38) 116.7 (7) C(28)-C(29)-C(30)-O(2) -142 (1) C(37)-C(38)-C(39) 122.5 (7) C(29)-C(30)-O(2)-Me(l) -179 (1) C(38)-C(39)-C(40) 119.2 (7) C(17)-C(31)-C(32)-C(33) -170 (1) C(39)-C(40)-C(35) 121.2 (7) C(31)-C(32)-C(33)… Show more

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Cited by 216 publications
(87 citation statements)
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“…The same situation was observed in a small molecule analogue, the para-nitrothiophenol thiolate complex of ferric protoporphyrin IX (FePSNP), reported by Tang et al (34). In P450-CAM, the S γ atom of the proximal cysteine is somewhat displaced off from the heme center and the S γ -Fe 3+ bonds form angles of 83° and 82° (in the two molecules of the unit cell) to the porphyrin plane.…”
Section: Structure Of Ferric H93g·bme Mb and Comparison With Cytochrosupporting
confidence: 70%
“…The same situation was observed in a small molecule analogue, the para-nitrothiophenol thiolate complex of ferric protoporphyrin IX (FePSNP), reported by Tang et al (34). In P450-CAM, the S γ atom of the proximal cysteine is somewhat displaced off from the heme center and the S γ -Fe 3+ bonds form angles of 83° and 82° (in the two molecules of the unit cell) to the porphyrin plane.…”
Section: Structure Of Ferric H93g·bme Mb and Comparison With Cytochrosupporting
confidence: 70%
“…While the complex was high-spin at room temperature, the EPR evidence indicates that the complex shifts to a low-spin complex in the frozen state at 77 K. In DMF, the complex shifts completely to the lowspin complex with g-values of 2.41, 2.27 and 1.93, which is similar to the g-values of other ferric porphyrins with thiolate ligands (Fe(OEP)(SPh)(DMF): 2.42, 2.27 and 1.92 [43]). The intensity of the high-spin EPR signal decreased linearly with the concentration of thiosulfate, reaching zero intensity with a 1:1 ferric porphyrin/thiosulfate ratio.…”
supporting
confidence: 59%
“…2A) is selectively perturbed in the Fe(III) G117I CooA variant. The rhombicity (expressed as E/D (26)) of G117I CooA is comparable to that of a model heme-thiolate complex (Table II ( 27)), although it is a bit lower than those of Fe(III) fivecoordinate, high spin thiolate-ligated hemoproteins such as cytochrome P450cam (P-450cam (28)), endothelial nitric oxide synthase (26), and chloroperoxidase (29) (Table II). On the other hand, the rhombicity of G117I CooA is significantly higher than those of nitrogen-based ligand high spin signal such as FixL (30) and soluble guanylyl cyclase (31).…”
Section: Ligation Structure and In Vivo Activity Of Glymentioning
confidence: 88%