You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Model Compounds for the T State of Hemoglobin
James P. Collman, John I. Brauman, Kenneth M. Doxsee, Thomas R. Halbert and Kenneth S. Suslick
Proceedings of the National Academy of Sciences of the United States of America
Vol. 75, No. 2 (Feb., 1978), pp. 564-568
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/67825
Page Count: 5
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
O2 binding to a series of ferrous and cobaltous ``picket fence'' porphyrins is reported. N-Methylimidazole and covalently attached imidazoles give O2 binding to ferrous porphyrins with Δ H degrees = -16.2 kcal/mol (-67.7 kJ/mol) and Δ S degrees = -40 eu (standard state, 1 atmosphere O2). Similar studies with cobaltous porphyrins yield Δ H degrees = -12.8 kcal/mol (-53.5 kJ/mol) and Δ S degrees = -39 eu. These values match well those of myoglobin and isolated subunits of hemoglobin and their cobalt reconstituted analogues. 1,2-Dimethylimidazole has been successfully used to mimic the presumed restraint of T state hemoglobin. In direct analogy to the decreased cooperativity shown by cobalt-substituted hemoglobin, model cobalt porphyrins show a smaller decrease in O2 affinity than the analogous iron porphyrins when the axial base is hindered. Thermodynamic data are presented. The molecular mechanism of cooperativity in hemoglobin is discussed.
Proceedings of the National Academy of Sciences of the United States of America © 1978 National Academy of Sciences