| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152545 | Journal of Inorganic Biochemistry | 2017 | 10 Pages |
Abstract
The C. diphtheriae heme uptake protein HtaA-CR2 has an axial tyrosine. Reconstitution with hemin after unfolding gave a different form of the protein, as revealed by UV-visible and Raman spectroscopy. Thermal and chemical unfolding experiments showed that hemin plays a significant role in the stability of the protein.207
Keywords
PMSFESIGdnHClFPLCHSAIPTGABC transporterDMSOhuman serum albuminSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisisopropyl β-D-1-thiogalactopyranosideCharge-transferELISAEnzyme-linked immunosorbent assayATP-binding cassette transporterDimethyl sulfoxideRamancircular dichroismcolumn volumefast protein liquid chromatographyterrific brothResonance Raman spectroscopyPhenylmethanesulfonyl fluorideconserved regioncarbon monoxidewild-typeHaptoglobinHemeHemoglobinHeminGuanidinium hydrochlorideHigh spinLow-spinCorynebacteriumGuanidiniumelectrospray ionization
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Rizvan C. Uluisik, Neval Akbas, Gudrun S. Lukat-Rodgers, Seth A. Adrian, Courtni E. Allen, Michael P. Schmitt, Kenton R. Rodgers, Dabney W. Dixon,