publication . Article . 2011

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Satoshi Nagao; Osamu Asami; Hiroyuki Yasui; Shun Hirota;
Open Access English
  • Published: 21 Jan 2011
  • Publisher: Elsevier
Abstract
Abstract Human myoglobin (hMb) possesses a cysteine (Cys) residue which is rare among mammalian Mbs. To investigate the effects of this unique Cys residue at the amino acid position 110 (Cys110) on hMb reactions, we studied the reactions of wild type (WT) met hMb and its alanine mutant at Cys110 (C110A) with H 2 O 2 , particularly in the presence of reduced glutathione (GSH) which is well known as a reducing agent. The formation rates of the ferryloxo (Fe(IV) = O) species by H 2 O 2 under air were about the same for WT and C110A met hMbs, whereas the protein decomposed more in the case of WT than C110A hMb. With the addition of GSH, hMb consumed H 2 O 2 faster a...
Subjects
Medical Subject Headings: skin and connective tissue diseaseshuman activities
free text keywords: Human myoglobin, Biophysics, Analytical Chemistry, Biochemistry, Molecular Biology, Radical, Myoglobin, chemistry.chemical_compound, chemistry, Amino acid, chemistry.chemical_classification, Reducing agent, Glutathione, Cysteine, Hydrogen peroxide, Alanine
Powered by OpenAIRE Open Research Graph
Any information missing or wrong?Report an Issue
publication . Article . 2011

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Satoshi Nagao; Osamu Asami; Hiroyuki Yasui; Shun Hirota;