publication . Article . 2011

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Nagao, Satoshi; Asami, Osamu; Yasui, Hiroyuki; Hirota, Shun;
Open Access English
  • Published: 21 Jan 2011
  • Publisher: Elsevier
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) methMb and its alanine mutant at Cys110 (C110A) with H2O2, 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 H2O2 under air were about the same for WT and C110A methMbs, whereas the protein decomposed more in the case of WT than C110A hMb. With the addition of GSH, hMb consumed H2O2 faster and decomposition of t...
Subjects
mesheuropmc: skin and connective tissue diseaseshuman activities
free text keywords: Human myoglobin
Download from
JAIRO
Article . 2011
Provider: JAIRO
Powered by OpenAIRE Open Research Graph
Any information missing or wrong?Report an Issue