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Journal of Biological Inorganic Chemistry

Volumn 16, Issue 4, 2011, Pages 599-609

A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification

(3) Igarashi, Jotaro a Kobayashi, Kazuo b Matsuoka, Ariki c

a TOHOKU UNIVERSITY (Japan)

b OSAKA UNIVERSITY (Japan)

c FUKUSHIMA MEDICAL UNIVERSITY (Japan)

Author keywords

Crystal structure; Nitric oxide detoxification; Tetrahymena pyriformis; Truncated hemoglobin

Indexed keywords

FERRIC ION; FERROUS ION; GLUTAMINE; NITRIC OXIDE; OXYGEN; TRUNCATED HEMOGLOBIN; TYROSINE; WATER;

AMINO ACID SEQUENCE; ARTICLE; AUTOOXIDATION; BINDING KINETICS; COMPLEX FORMATION; CRYSTAL STRUCTURE; DETOXIFICATION; DISSOCIATION CONSTANT; HYDROGEN BOND; MYCOBACTERIUM TUBERCULOSIS; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STABILITY; TETRAHYMENA PYRIFORMIS;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GLUTAMINE; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; NITRIC OXIDE; OXIDATION-REDUCTION; OXYGEN; RECOMBINANT PROTEINS; TETRAHYMENA PYRIFORMIS; TRUNCATED HEMOGLOBINS; TYROSINE;

CILIOPHORA; MYCOBACTERIUM TUBERCULOSIS; PROTISTA; TETRAHYMENA; TETRAHYMENA PYRIFORMIS;

EID: 79955783127 PISSN: 09498257 EISSN: None Source Type: Journal
DOI: 10.1007/s00775-011-0761-3 Document Type: Article

Times cited : (27)

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