Functional importance of tyrosine 294 and the catalytic selectivity for the Bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine

Biochemistry

Volumn 49, Issue 45, 2010, Pages 9783-9791

  Abu Tarboush, Nafez ^a   Jensen, Lyndal M R ^a   Feng, Manliang ^a   Tachikawa, Hiroyasu ^c   Wilmot, Carrie M ^b   Davidson, Victor L ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

^b UNIVERSITY OF MINNESOTA   (United States)

^c JACKSON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AXIAL LIGAND; AXIAL LIGATION; BINDING PROPERTIES; COFACTORS; COMPOUND I; DIRECT CONTACT; ELECTRON TRANSFER; HEME IRON; LONG-RANGE ELECTRON TRANSFER; METHYLAMINE DEHYDROGENASE; POST-TRANSLATIONAL MODIFICATIONS; PRECURSOR PROTEINS; REDOX PROPERTY; REDOX STATE; SPECTROSCOPIC DATA; TWO-ELECTRON OXIDATION; WILD TYPES;

AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; CRYSTAL STRUCTURE; ELECTRON TRANSITIONS; FREE RADICAL REACTIONS; LIGANDS; REACTION INTERMEDIATES; REDOX REACTIONS;

PORPHYRINS;

AMINE DEHYDROGENASE; BISMUTH; HEME; HISTIDINE; IRON; LIGAND; TRYPTOPHAN; TYROSINE;

ARTICLE; BIOSYNTHESIS; CATALYSIS; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; GENE MUTATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN SYNTHESIS; REDOX STRESS; SPECTROSCOPY; WILD TYPE;

FERRIC COMPOUNDS; FERROUS COMPOUNDS; HEME; HISTIDINE; LIGANDS; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PROTEIN CONFORMATION; PROTEIN PRECURSORS; QUINOLINES; SMAD1 PROTEIN; SPECTRUM ANALYSIS, RAMAN; TYROSINE;

EID: 78149421684     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101254p     Document Type: Article

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