Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands

Biochemistry

Volumn 48, Issue 49, 2009, Pages 11603-11605

  Fu, Rong ^a,c   Liu, Fange ^a   Davidson, Victor L ^b   Liu, Aimin ^a  

^a GEORGIA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

^c EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC MECHANISMS; COFACTORS; ELECTRON TRANSFER; ELECTRONIC COMMUNICATIONS; EPR SPECTRA; EXOGENOUS LIGANDS; HEME IRON; IRON CENTERS; METHYLAMINE DEHYDROGENASE; NITROSYL COMPLEX; PORPHYRIN CATIONS; REDOX EQUILIBRIUM; REDOX STATE; TRYPTOPHAN RESIDUES; TWO-ELECTRON OXIDATION;

AMINO ACIDS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYMES; FREE RADICAL REACTIONS; HEMOGLOBIN; IRON COMPOUNDS; LIGANDS; NITRIC OXIDE; OXYGEN; STRONTIUM COMPOUNDS;

PORPHYRINS;

HEME; HISTIDINE; IRON; LIGAND; MAUG PROTEIN; NITRIC OXIDE; PORPHYRIN; UNCLASSIFIED DRUG;

ARTICLE; BEHAVIOR; CATALYSIS; CHEMICAL STRUCTURE; ELECTRON TRANSPORT; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN BINDING;

BACTERIAL PROTEINS; CATALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; FERRIC COMPOUNDS; HEME; HEMEPROTEINS; IRON; LIGANDS; NITROGEN OXIDES; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PROTEIN BINDING;

EID: 71549131616     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9017544     Document Type: Article

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