Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 24, 2013, Pages 9639-9644

  Geng, Jiafeng ^a   Dornevil, Kednerlin ^a   Davidson, Victor L ^b   Liu, Aimin ^a  

^a GEORGIA STATE UNIVERSITY   (United States)

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

Author keywords

Charge transfer; Electron hopping; High valent iron; Metalloprotein; Tryptophan radical

Indexed keywords

HEME; IRON DERIVATIVE; MAUG PROTEIN; OXIDIZING AGENT; TRYPTOPHAN; UNCLASSIFIED DRUG;

ABSORPTION; ARTICLE; ELECTRON TRANSPORT; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME STABILITY; ENZYME STRUCTURE; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; OXIDATIVE COUPLING; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

CHARGE TRANSFER; ELECTRON HOPPING; HIGH-VALENT IRON; METALLOPROTEIN; TRYPTOPHAN RADICAL;

CATALYSIS; ENZYME PRECURSORS; FERRIC COMPOUNDS; HEME; HEMEPROTEINS; HISTIDINE; INDOLEQUINONES; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SPECTROSCOPY, NEAR-INFRARED; TRYPTOPHAN; TYROSINE;

EID: 84878986117     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1301544110     Document Type: Article

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