Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
作者:, Michael T. Wilson
摘要:Abstract 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 have unequivocally assigned CO binding to hexa- and penta-coordinate forms and have made direct measurement of histidine rebinding following photolysis. We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding.
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论文方向:[{"id":13,"name":"细胞生物学"},{"id":879,"name":"生物化学"}]
发表期刊:FEBS Letters Volume 589, Issue 4
发表时间:Fri Feb 13 00:00:00 CST 2015
数字识别码:10.1016/j.febslet.2015.01.010
是否作者本人: 否
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