Ligand binding to heme proteins. An evaluation of distal effects.

  title={Ligand binding to heme proteins. An evaluation of distal effects.},
  author={Martha P. Mims and Arturo G Porras and John S Olson and Robert W. Noble and Julian Peterson},
  journal={The Journal of biological chemistry},
  volume={258 23},
The O2, CO, and alkyl isocyanide-binding properties of a variety of vertebrate and invertebrate heme proteins have been compared in detail to those of protoheme mono-3-(1-imidazoyl)-propylamide monomethyl ester in aqueous suspensions of soap micelles. The proteins examined include: cytochrome P-450cam from Pseudomonas putida, beef heart cytochrome c oxidase, yeast cytochrome c peroxidase, alpha and beta subunits of human hemoglobin, sheep hemoglobin, carp hemoglobin, sperm whale myoglobin… CONTINUE READING
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