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Hunsicker-Wang, Laura M. ; Vogt, Matthew J. ; Hoogstraten, Charles G. ; Cosper, Nathaniel J. ; Davenport, Audrey M. ; Hendon, Christopher H. ; Scott, Robert A. ; Britt, R. David ; DeRose, Victoria J. ( , Journal of Inorganic Biochemistry)
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Lopez, Liezelle C. ; Mukhitov, Nikita ; Handley, Lindsey D. ; Hamme, Cristina S. ; Hofman, Cristina R. ; Euers, Lindsay ; McKinney, Jennifer R. ; Piers, Amani D. ; Wadler, Ellen ; Hunsicker‐Wang, Laura M. ( , Protein Science)
Abstract The Sco protein from
Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuAprotein fromT. thermophilus , which is a soluble protein engineered from subunit II of cytochromeba 3 oxidase that lacks the transmembrane helix. The native cysteines onTt Sco andTt CuAwere mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine inTt CuAand subsequent release upon incubation with the complementaryTt Sco protein demonstrated the formation of the mixed disulfide intermediate. The cysteine ofTt Sco that attacks the disulfide bond in the targetTt CuAprotein was determined to beTt Sco Cysteine 49. This cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+or Cu+toTt Sco prior to reaction withTt CuAwas found to preclude formation of the mixed disulfide intermediate. These results shed light on a mechanism of disulfide bond reduction by theTt Sco protein and may point to a possible role of metal binding in regulating the activity.Importance The function of Sco is at the center of many studies. The disulfide bond reduction in CuAby Sco is investigated herein and the effect of metal ions on the ability to reduce and form a mixed disulfide intermediate are also probed.