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- W2899080552 abstract "Cytoglobin (Cygb) is a highly conserved, hexacoordinate heme protein expressed ubiquitously in mammalian tissues. Unlike other commonly found globins (i.e., hemoglobin and myoglobin), Cygb has a bound - but dissociable - proximal histidine that hinders ligand binding and, unlike the common globins, Cygb is not regarded to be closely associated with oxygen transport. The physiological functions of Cygb are still unclear but are thought to include ROS detoxification, lipid peroxidation, and vascular nitric oxide metabolism via hypoxic nitrite reduction and O2-dependent nitric oxide dioxygenation. All of these processes first require dissociation of the distal histidine to generate an active penta-coordinate heme. Further, these processes are likely further modulated by two conserved cysteine residues (Cys38 and Cys83), which can readily generate intermolecular dimeric and intramolecular monomeric disulfide bonds. For instance, formation of the intramolecular monomer greatly increases the nitrite reductase (NiR) activity, suggesting a change in pocket shape resulting in an increase in the rate and frequency the distal histidine dissociates. Predominantly using stopped-flow and kinetic techniques, we are assessing the effect of the redox states of these cysteines via small molecule binding/reaction characterization in both the ferrous and ferric form of the protein, elucidating differences in the binding pocket conformation in various redox environments. These methodologies consequently allow for the assessment of the thiol oxidation state, as different preparations of recombinant Cygbs vary and result in formation of differing cysteine redox states. Chemical modification and point mutations have been used to generate a number of modified cytoglobins to develop a more complete picture of the effect of the redox states of these cysteines." @default.
- W2899080552 created "2018-11-09" @default.
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- W2899080552 date "2018-11-01" @default.
- W2899080552 modified "2023-09-26" @default.
- W2899080552 title "Interrogating the cytoglobin binding pocket and thiol redox status with point mutations and chemical probes" @default.
- W2899080552 doi "https://doi.org/10.1016/j.freeradbiomed.2018.10.086" @default.
- W2899080552 hasPublicationYear "2018" @default.
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