Detail of "21007-21-6"

Reference

Determination of the molar extinction coefficients of the deuteroferriheme analogs of peroxidase enzyme compounds I and II

Determination of the molar extinction coefficients of the deuteroferriheme analogs of peroxidase enzyme compounds I and II. Woo, Fanny S.; Rodriguez, Ricardo E.; Huckaby, Dale A.; Jones, Peter; Kelly, Henry C. (Dep. Chem., Texas Christian Univ., Fort Worth, TX 76129, USA). Inorg. Chem., 31(7), 1144-7 (English) 1992. CODEN: INOCAJ. ISSN: 0020-1669. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Absorbance data obtained in the stopped-flow spectrophotometric study of the in situ biphasic regeneration of deuteroferriheme (dfh) following its oxidn. by NaOCl were utilized to calc. extinction coeffs. of species presumed to be involved in series pseudo-1st-order redox regeneration processes. Such data were interpreted in terms of a previously proposed mechanism of the type A ? B ? C where A denotes the dfh-OCl- oxidn. product; B, a reaction intermediate; and C, the regenerated dfh. The results were consistent with a scheme involving consecutive 1-electron redns. of the heme analogs of peroxidase compds. I and II to regenerate free dfh in a state of monomer-dimer equil. A value e x 4M-1 cm-1 at l = 384 nm was computed at pH 6.85 and 25° for the molar extinction coeff. of the compd. II analog (B), which was depicted as dinuclear FeIIIOFeIV. This was intermediate in magnitude between the value e x 2 ′ 104M-1 cm-1 calcd. for the dfh-derived compd. I analog (A), depicted as FeIV2O, and previously calcd. values of extinction coeffs. for monomeric and dimeric dfh.In this experiment, several chemicals are used like 9003-99-0 and 21007-21-6 Such e values were consistent with obsd. changes in optical d. accompanying heme regeneration and with kinetic studies. .

Characterization of the electrochemical behavior of the prosthetic group of hemoproteins

Characterization of the electrochemical behavior of the prosthetic group of hemoproteins. I. Direct and alternating current polarography of deuterohemin. Scheller, F.; Pruemke, H. J.; Mohr, P.; Seyer, I.; Makower, A.Chemicals with cas numbers 21007-21-6 and 448-65-7 also play role. (Zentralinst. Molekularbiol., DAW, Berlin, E. Ger.). Stud. Biophys., 62(3), 223-31 (German) 1977. CODEN: STBIBN. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) The redox behavior of deuterohemin was studied by d.c. and a.c. polarog. Adsorption kinetics indicated that the deuterohemin is arranged on the electrode in a flat position. The reversible redn. of both the central atom and the porphyrin ring yields peaks in a.c. polarograms. The origin of concn. dependence of the peak at the redox potential of the hemin-heme system is discussed with ref. to a redn. of the 2nd adsorption layer or a monomer-dimer equil. in soln. .