The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c-550 from Paracoccus versutus assessed by X-ray crystallography and unfolding

FEBS Journal

Volumn 272, Issue 10, 2005, Pages 2441-2455

  Worrall, Jonathan A R ^a   Van Roon, Anne Marie M ^a   Ubbink, Marcellus ^a   Canters, Gerard W ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

Author keywords

Axial ligand; Cytochrome c; Unfolding, peroxidase activity; X ray crystallography

Indexed keywords

CYTOCHROME C; CYTOCHROME C550; HEME; IRON; LIGAND; LYSINE; METHIONINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; DISSOCIATION; ENZYME CONFORMATION; ENZYME STRUCTURE; FREEZING; HYDROGEN BOND; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PARACOCCUS VERSUTUS; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; WILD TYPE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME C GROUP; ENZYME STABILITY; HEME; LIGANDS; LYSINE; METHIONINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARACOCCUS; PEROXIDASES; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE;

BACTERIA (MICROORGANISMS); PARACOCCUS VERSUTUS;

EID: 18944402348     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04664.x     Document Type: Article

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