Cu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopA

FEBS Journal

Volumn 279, Issue 2, 2012, Pages 285-298

  Zhou, Liang ^a   Singleton, Chloe ^a   Hecht, Oliver ^a   Moore, Geoffrey R ^a   Le Brun, Nick E ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

Bacillus subtilis; copper exchange; copper trafficking; cysteine thiol; P type ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; COPPER ION; CYSTEINE; PROTON;

AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; BACILLUS SUBTILIS; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; DIMERIZATION; ENZYME BINDING; ENZYME ISOLATION; ENZYME PURIFICATION; EXPRESSION VECTOR; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN UNFOLDING; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; ALGORITHMS; AMINO ACID MOTIFS; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CATION TRANSPORT PROTEINS; CHELATING AGENTS; COPPER; CYSTEINE; DIMERIZATION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; PROTONS; RECOMBINANT PROTEINS; SOLUBILITY;

BACILLUS SUBTILIS; EUKARYOTA; PROKARYOTA;

EID: 84855467545     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08422.x     Document Type: Article

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