Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity

FEBS Letters

Volumn 586, Issue 24, 2012, Pages 4339-4343

  Abu Tarboush, Nafez ^a   Shin, Sooim ^b   Geng, Jiafeng ^c   Liu, Aimin ^c   Davidson, Victor L ^b  

^a UNIVERSITY OF JORDAN   (Jordan)

^b UNIVERSITY OF CENTRAL FLORIDA COLLEGE OF MEDICINE   (United States)

^c GEORGIA STATE UNIVERSITY   (United States)

Author keywords

Cytochrome c; High valence Fe; Redox enzyme; Tryptophan tryptophylquinone

Indexed keywords

AMINE DEHYDROGENASE; BACTERIAL ENZYME; ENZYME VARIANT; HEME; LIGAND; LYSINE; PEROXIDE; PROTEIN MAUG; TRYPTOPHAN DERIVATIVE; TRYPTOPHAN TRYPTOPHYLQUINONE COFACTOR; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BIOSYNTHESIS; CHEMICAL REACTION; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME MODIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; OXIDATION REDUCTION STATE; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN PROCESSING;

BACTERIAL PROTEINS; HEME; HEMEPROTEINS; HISTIDINE; INDOLEQUINONES; LIGANDS; LYSINE; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PARACOCCUS DENITRIFICANS; PEROXIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; SPECTROPHOTOMETRY; TRYPTOPHAN; TYROSINE;

EID: 84870509485     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.10.044     Document Type: Article

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