Modulation of cooperativity in Mycobacterium tuberculosis NADPH-ferredoxin reductase: Cation- and pH-induced alterations in native conformation and destabilization of the NADP+-binding domain

Protein Science

Volumn 14, Issue 4, 2005, Pages 980-992

  Bhatt, Anant Narayan ^a   Shukla, Nidhi ^a   Aliverti, Alessandro ^b   Zanetti, Giuliana ^b   Bhakuni, Vinod ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

^b UNIVERSITY OF MILAN   (Italy)

Author keywords

Cation; Cooperativity; Flavoprotein; Mycobacterium tuberculosis; Thermal denaturation

Indexed keywords

APOENZYME; BACTERIAL ENZYME; CALCIUM CHLORIDE; CATION; DIVALENT CATION; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; FPRA PROTEIN; MAGNESIUM CHLORIDE; MONOVALENT CATION; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; POTASSIUM CHLORIDE; QUERCETIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ACIDITY; AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENOME; BINDING SITE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME MODIFICATION; ENZYME STABILITY; HEAT TREATMENT; MOLECULAR INTERACTION; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PH; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; REGULATORY MECHANISM; SEQUENCE ANALYSIS; THERMOSTABILITY;

CALCIUM CHLORIDE; CATIONS; FERREDOXIN-NADP REDUCTASE; HYDROGEN-ION CONCENTRATION; NADH, NADPH OXIDOREDUCTASES; NADP; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SODIUM CHLORIDE; TEMPERATURE;

EID: 15244354166     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041162705     Document Type: Article

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