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- W2070296883 abstract "The spectroscopic responses of Rhodospirillum rubrum haem protein to a variety of ligands over the pH range 5.2–12 have been examined. Only small uncharged molecules, e.g., NO and CO, are able to penetrate to the prosthetic haem groups of the protein. NO reacts not as a ligand, however, but causes changes which appear to be the result of oxidative alterations either of the porphyrin moeities or a reactive groups in the immediate peptide environment, or of both. CO, on the other hand, reacts as a true ligand. However, the affinity of rhodospirillum haem protein for CO is much less than that of most other haem proteins; the half-saturation value for ferro-rhodospririllum haem protein-CO formation is about 0.015 atm at all pH values tested. The atypical variation in photodissociability of ferro-rhodospirillum haem protein-CO with pH, noted previously, is confirmed." @default.
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- W2070296883 date "1963-01-01" @default.
- W2070296883 modified "2023-09-27" @default.
- W2070296883 title "On the anomalous interactions of ligands with rhodospirillum haem protein" @default.
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- W2070296883 doi "https://doi.org/10.1016/0006-3002(63)91387-8" @default.
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