Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin

Biochemistry

Volumn 37, Issue 19, 1998, Pages 7047-7056

  Tang, Qun ^a   Kalsbeck, William A ^a   Olson, John S ^b   Bocian, David F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b RICE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; GUANIDINE; HEME; HISTIDINE; IRON; ISOLEUCINE; LEUCINE; METMYOGLOBIN; MUTANT PROTEIN; MYOGLOBIN; PHENYLALANINE; VALINE;

ABSORPTION SPECTROSCOPY; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL BINDING; DISSOCIATION; EQUILIBRIUM CONSTANT; LIGAND BINDING; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; SOLVATION; WHALE;

ACIDS; ANIMALS; GUANIDINE; HEME; HISTIDINE; HYDROGEN-ION CONCENTRATION; IRON; KINETICS; MALE; MUTAGENESIS, SITE-DIRECTED; MYOGLOBIN; PROTEIN FOLDING; SPECTROPHOTOMETRY; SPERMATOZOA; WHALES;

CETACEA; PHYSETER CATODON;

EID: 0032510761     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9729413     Document Type: Article

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