32464-39-4Relevant articles and documents
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Parker,Brinigar
, p. 325,326-328 (1976)
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Syntheses of Methyl-devinylporphyrins Related to Protoporphyrin -IX. Initial Studies on the Mechanism of the Copper(II) Catalysed Cyclization of 1',8'-Dimethyl-a,c-biladiene Salts
Smith, Kevin M.,Kehres, Lisa A.
, p. 2329 - 2335 (2007/10/02)
Using copper(II) catalysed cyclization of a,c-biladiene dihydrobromide salts, porphyrins related to protoporphyrin-IX dimethyl ester (8), but in which both vinyls are replaced with methyls, or where either the 2- or 4-vinyls are individually replaced with methyls, are synthesized.These compounds are required for reconstitution of the corresponding hemes into hemoproteins, to enable the study of the rotational disorder of prosthetic heme groups in reconstituted hemoproteins.By way of 13C n.m.r. spectroscopy of enriched a,c-biladienes and porphyrins, the copper(II) catalysed cyclization of 1',8'-dimethyl-a,c-biladiene dihydrobromides is shown to afford porphyrins in which one of the 1'- and 8'-methyl groups becomes the new linking meso carbon atom.
Electronic and steric factors affecting ligand binding: horse hemoglobins containing 2,4 dimethyldeuteroheme and 2,4 dibromodeuteroheme
Seybert,Moffat,Gibson,Chang
, p. 4225 - 4231 (2007/10/09)
Horse globin has been recombined with 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme to yield the corresponding reconstituted hemoglobins, and the ligand binding reactions of these reconstituted hemoglobins have been examined in detail. Both hemoglobins exhibit relatively high n values, but 2,4-dimethyldeuterohemoglobin displays a consistently higher oxygen affinity than native hemoglobin, whereas the oxygen affinity of 2,4-dibromodeuterohemoglobin is consistently lower than that of native hemoglobin. The rate constants 1'1 and 1'4 for the binding of the first and fourth molecules of CO, respectively, for both reconstituted hemoglobins are not markedly different from those of native hemoglobin. In contrast, the kinetic rate constants for oxygen dissociation from these hemoglobins are appreciably altered. The rate constants for oxygen dissociation in the presence of dithionite for 2,4-dimethyl- and 2,4-dibromodeuterohemoglobin are 8 s-1 and 72 s-1, respectively; the corresponding rate constant for native hemoglobin is 33 s -1. Analogous results were obtained for the dissociation of oxygen in the presence of dithionite and CO. The pK of the acid-alkaline transition in the Met forms of the two reconstituted hemoglobins (pK') was also appreciably different for 2,4-dimethyl- and 2,4-dibromodeuterohemoglobin. A linear free energy relationship was found between the logarithms of the rate constants for oxygen dissociation from various reconstituted hemoglobins and pK3 of the corresponding metal-free porphyrins. A similar relationship exists between pK' and pK3, although no apparent correlation was seen between the logarithms of the association rate constants for CO and pK3 of the porphyrins. The results indicate that the rate of oxygen dissociation from hemoglobin is strongly influenced by the strength of the iron-ligand bond. However, the rate of association of CO to hemoglobin is relatively insensitive to the strength of this bond, and is probably controlled by steric effects in the ligand pocket of hemoglobin.