Collman, James P. and Brauman, John I. and Doxsee, Kenneth M. (1979) Carbon monoxide binding to iron porphyrins. Proceedings of the National Academy of Sciences of the United States of America, 76 (12). pp. 6035-6039. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:COLpnas79
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The carbon monoxide affinities of iron complexes of meso-tetra (α,α,α,α-o-pivalamidophenyl)porphyrin (the "picket fence" porphyrin) and of a "picket fence" porphyrin derivative with an appended axial base have been measured in solution and compared with the CO affinities of various hemoproteins. The model complexes bind CO with much greater affinity than normal hemoproteins; the role of the steric bulk of distal residues in lowering the CO affinities of the hemoproteins is discussed. The significance of this lowered CO affinity is described with regard to endogenous CO. A discussion of mutant hemoglobins lacking distal residues that sterically inhibit the binding of CO is presented. The use of pressure units versus concentration units in equilibrium expressions is analyzed.
|Additional Information:||Copyright © 1979 by the National Academy of Sciences. Contributed by James P. Collman, July 23, 1979. We are grateful to Dr. K.S. Suslick for helpful criticism. We thank the National Science Foundation (Grant CHE78-09443) and the National Institutes of Health (Grant GM17880). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.|
|Subject Keywords:||picket fence porphyrins; hemoproteins; distal residues; partition coefficient; solvation|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||31 Jul 2007|
|Last Modified:||26 Dec 2012 09:34|
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