Cytoglobin conformations and disulfide bond formation
نویسندگان
چکیده
منابع مشابه
Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding.
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 ligands. Through time-resolved spectra we...
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The disposition and disposal of the -SH groups of the lens during aging and cataractogenesis have been investigated by laser Raman spectroscopy as a noninvasive microprobe in the intact living lens. In this procedure -SH and -S-S- give unique discrete Raman signals (at 2580 and 508 cm-1) that may be used to calculate relative concentrations in a very small volume of the lens. We present evidenc...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2010
ISSN: 1742-464X,1742-4658
DOI: 10.1111/j.1742-464x.2010.07686.x