Synthesis of the Myoglobin Active Site | Zendy

Chi K. Chang | Zendy; Teddy G. Traylor | Zendy

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Synthesis of the Myoglobin Active Site

Author(s) -

Chi K. Chang,

Teddy G. Traylor

Publication year - 1973

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.70.9.2647

Subject(s) - myoglobin , imidazole , heme , chemistry , hemeprotein , amide , active site , stereochemistry , combinatorial chemistry , organic chemistry , catalysis , enzyme

A simple heme-imidazole compound, having the same geometry as the heme-imidazole complex in myoglobin, has been synthesized. This compound, ferropyrroporphyrin-N -[3-(1-imidazolyl)propyl]amide, reversibly binds oxygen in the solid state or when dissolved in a polystyrene film. These results suggest that the principal factors governing reversible oxygen binding are the electronic nature of the base (imidazole), neighboring-group effects of the basic group, and immobilization of the heme group.

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