Resonance raman spectra of an O2-binding H-NOX domain reveal heme relaxation upon mutation

Biochemistry

Volumn 48, Issue 36, 2009, Pages 8568-8577

  Tran, Rosalie ^a   Boon, Elizabeth M ^a,b   Marletta, Michael A ^a   Mathies, Richard A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; CONFORMATIONAL HETEROGENEITY; CONSERVED RESIDUES; CRYSTAL FORMS; HIGH FREQUENCY; INCREASED FLEXIBILITY; LOW-FREQUENCY MODES; OUT-OF-PLANE; RAPID SAMPLING; RESONANCE RAMAN; RESONANCE RAMAN SPECTRA; STRETCHING MODES; UNIT CELLS; VIBRATIONAL FREQUENCIES; WILD TYPES;

CELL MEMBRANES; CHROMOPHORES; CONFORMATIONS; PORPHYRINS; RAMAN SCATTERING; RAMAN SPECTROSCOPY; RESONANCE;

HEMOGLOBIN;

HEME; NITRIC OXIDE; OXYGEN;

ARTICLE; CHROMATOPHORE; MUTATION; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; THERMOANAEROBACTER; THERMOANAEROBACTER TENGCONGENSIS;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; HEMEPROTEINS; ISOLEUCINE; LIGANDS; NITRIC OXIDE; OXYGEN; PROLINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS, RAMAN; THERMOANAEROBACTER;

THERMOANAEROBACTER TENGCONGENSIS;

EID: 70149124102     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900563g     Document Type: Article

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