O2-mediated oxidation of ferrous nitrosylated human serum heme-albumin is limited by nitrogen monoxide dissociation

Biochemical and Biophysical Research Communications

Volumn 406, Issue 1, 2011, Pages 112-116

  Ascenzi, Paolo ^a,b   Gullotta, Francesca ^c,d   Gioia, Magda ^c,d   Coletta, Massimo ^c,d   Fasano, Mauro ^e  

^a ROMA TRE UNIVERSITY   (Italy)

^b NATIONAL INSTITUTE FOR INFECTIOUS DISEASES L SPALLANZANI   (Italy)

^c UNIVERSITY OF ROME TOR VERGATA   (Italy)

^d Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems (CIRCMS   (Italy)

^e UNIVERSITY OF INSUBRIA   (Italy)

Author keywords

Allostery; Dioxygen mediated oxidation; Ferrous nitrosylated human serum heme albumin; Human serum albumin; Kinetics; Rifampicin

Indexed keywords

FERROUS ION; HEME; HEMIN; IRON DERIVATIVE; NITRIC OXIDE; OXYGEN; RIFAMPICIN; SERUM ALBUMIN;

ALBUMIN BLOOD LEVEL; ALLOSTERISM; ARTICLE; ATOM; DISSOCIATION; HUMAN; KINETICS; MODULATION; NITROSYLATION; OXIDATION; PRIORITY JOURNAL;

HEME; HUMANS; IRON; NITRIC OXIDE; OXIDATION-REDUCTION; OXYGEN; SERUM ALBUMIN;

EID: 79952191239     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.02.005     Document Type: Article

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