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JBC, Vol. 250, Issue 19, 7602-7622, Oct, 1975

Heme A of cytochrome c oxicase. Structure and properties: comparisons with hemes B, C, and S and derivatives

W. S. Caughey, G. A. Smythe, D. H. O'Keeffe, J. E. Maskasky and M. I. Smith

Heme A, isolated from bovine heart muscle by procedures which include extractions into pyridine/chloroform and two-phase, liquid-liquid chromatography on Celite, has been converted to several derivatives. Examination of the proton nuclear magnetic resonance (PMR) spectra and other properties of these derivatives reveals heme A to be the iron complex of 8-formyl-6,-m-bis(2''-hydroxycarbonylethyl)-2-(1'-hydroxy-5',9',13'-trimet hyl-4',8',12'-trans,trans-tetradecatrienyl)-1,3,5-trimethyl-4-vinylporphin . Substituents at the 2,4, and 8 positions are replaced by hydrogen in a resorcinol melt to give cytodeuteroporphin (8-demethyldeuteroporphyrin IX)...
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