WebSep 15, 2010 · Cytoglobin has the classical globin fold, with an extension at each extremity of about 20 residues. The e... Cytoglobin conformations and disulfide bond formation - Lechauve - 2010 - The FEBS Journal - Wiley Online Library WebNov 23, 2003 · Cytoglobin (Cgb), a newly discovered member of the vertebrate globin family, binds O(2) reversibly via its heme, as is the …
Characterization of the Heme Environmental Structure of Cytoglobin, a ...
WebApr 4, 2024 · A de novo designed intramolecular disulfide bond in myoglobin, resembling that in cytoglobin without structural evidence, was confirmed by an X-ray structure for the first time and was demonstrated to regulate both the structure and function of this protein, which fulfills the design of an artificial dehaloperoxidase, with an activity exceeding … WebStructural effects of disulfide bond formation in Cytoglobin. The crystal structure of wild-type Cygb without the intramolecular disulfide bond (top left) and a model for the structure with the intramolecular disulfide bond (top right) are shown . how to run .cu file in windows
Allosteric Regulation and Temperature Dependence of Oxygen …
WebFeb 13, 2015 · Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38–C83) alters the dissociation rate constant of the intrinsic histidine (H81) (∼1000 fold), thus controlling binding of extrinsic … WebFeb 16, 2012 · Cytoglobin is an intracellular globin of unknown function that is expressed mostly in cells of a myofibroblast lineage. Possible functions of cytoglobin include buffering of intracellular oxygen and detoxification of reactive oxygen species. WebSep 15, 2010 · Cygb is considered to be in a clade with vertebrate myoglobin (Mb) and shares about 30% amino acid sequence identity with Mb, implying a common evolutionary ancestry [ 3 ]. Human Cygb is … northern region of saudi arabia