Sulfide binding properties of truncated hemoglobins

Biochemistry

Volumn 49, Issue 10, 2010, Pages 2269-2278

  Nicoletti, Francesco P ^b   Comandini, Alessandra ^a   Bonamore, Alessandra ^a   Boechi, Leonardo ^c   Boubeta, Fernando Martin ^c   Feis, Alessandro ^b   Smulevich, Iulietta ^b   Boffi, Alberto ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF FLORENCE   (Italy)

^c Instituto de Quimica Fisica de los Materiales Medio Ambiente y Energia   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS SUBTILIS; BEARING-ONLY; BINDING PARAMETER; BINDING PROPERTIES; BOUND LIGANDS; CLASSICAL MOLECULAR DYNAMICS; CYSTEINE BIOSYNTHESIS; ESCHERICHIA COLI CELLS; EXPERIMENTAL DATA; FERRIC IRON; HIGH AFFINITY; HYDROGEN BONDING STABILIZATION; KINETIC BARRIER; KINETIC STUDY; LUCINA PECTINATA; ORDER OF MAGNITUDE; OVER-EXPRESSION; PARTIALLY SATURATED; RECOMBINANT PROTEIN; RESONANCE RAMAN SPECTROSCOPY; SECOND-ORDER RATE CONSTANTS; STRETCHING BANDS; SULFIDE SPECIES; THERMOBIFIDA FUSCA; TRUNCATED HEMOGLOBINS; WILD-TYPE PROTEINS;

BACTERIOLOGY; BINDING ENERGY; BIOCHEMISTRY; COORDINATION REACTIONS; ESCHERICHIA COLI; HEMOGLOBIN; HYDROGEN; HYDROGEN BONDS; MOLECULAR DYNAMICS; RAMAN SPECTROSCOPY; RATE CONSTANTS; SPIN DYNAMICS; STABILIZATION; SULFUR DETERMINATION;

HYDROGEN SULFIDE;

BACTERIAL PROTEIN; CYSTEINE; FERRIC ION; HYDROGEN SULFIDE; RECOMBINANT PROTEIN; TRUNCATED HEMOGLOBIN;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL CELL; BACTERIUM; BINDING AFFINITY; BIOSYNTHESIS; ESCHERICHIA COLI; HOMEOSTASIS; HYDROGEN BOND; KINETICS; MOLECULAR DYNAMICS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; RAMAN SPECTROMETRY; THERMOBIFIDA FUSCA; THERMODYNAMICS;

ACTINOMYCETALES; BACILLUS SUBTILIS; BACTERIAL PROTEINS; KINETICS; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFIDES; THERMODYNAMICS; TRUNCATED HEMOGLOBINS;

BACILLUS SUBTILIS; ESCHERICHIA COLI; LUCINA PECTINATA; THERMOBIFIDA FUSCA;

EID: 77949408968     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901671d     Document Type: Article

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