The coordination of Ni II and Cu II ions to the polyhistidyl motif of Hpn protein: Is it as strong as we think?

Chemistry - A European Journal

Volumn 18, Issue 35, 2012, Pages 11088-11099

  Witkowska, Danuta ^a   Politano, Rossella ^b   Rowinska Zyrek, Magdalena ^a   Guerrini, Remo ^b   Remelli, Maurizio ^b   Kozlowski, Henryk ^a  

^a UNIVERSITY OF WROC AW   (Poland)

^b UNIVERSITY OF FERRARA   (Italy)

Author keywords

coordination modes; copper; histidine; nickel; proteins

Indexed keywords

BINDING INTERACTION; BIOINORGANIC CHEMISTRY; COORDINATION MODES; HELICOBACTER PYLORI; HISTIDINE; ION BINDING; NATURALLY OCCURRING; SPECTROSCOPIC TECHNIQUE; WILD TYPES;

AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; COPPER; NICKEL;

PROTEINS;

ALANINE; BACTERIAL PROTEIN; COORDINATION COMPOUND; COPPER; HISTIDINE; NICKEL; POLYHISTIDINE; TYROSINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HELICOBACTER PYLORI; KINETICS; MASS SPECTROMETRY; MOLECULAR GENETICS; PH; POTENTIOMETRY; PROTEIN BINDING; SYNTHESIS;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; COORDINATION COMPLEXES; COPPER; HELICOBACTER PYLORI; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NICKEL; POTENTIOMETRY; PROTEIN BINDING; TYROSINE;

EID: 84865201817     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.201200780     Document Type: Article

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