High-resolution X-ray structures of myoglobin- and hemoglobin-alkyl isocyanide complexes
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The structures of sperm whale myoglobin (Mb) and human hemoglobin (Hb) complexed with methyl, ethyl, n-propyl and n-butyl isocyanide (MNC, ENC, nPNC and nBNC, respectively) were determined by X-ray crystallography. The polar isocyano head groups of the alkyl isocyanides (RNC's) have similar affinities for heme iron, whereas the size and stereochemistry of the alkyl groups cause the different RNC ligands to cross varied steric barriers when entering or exiting the protein. Four Mb structures were determined at a resolution $$ 100
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Johnson, Kenneth Alan. "High-resolution X-ray structures of myoglobin- and hemoglobin-alkyl isocyanide complexes." (1993) Diss., Rice University. https://hdl.handle.net/1911/16633.