Title
Spectral characterization of the recombinant mouse tumor suppressor 101F6 proteinSpectral characterization of the recombinant mouse tumor suppressor 101F6 protein
Author
Faculty/Department
Faculty of Sciences. Biology
Faculty of Sciences. Physics
Research group
Integrated Molecular Plant Physiology Research (IMPRES)
Molecular Plant Physiology and Biotechnology
Biophysics and Biomedical Physics
Publication type
article
Publication
Berlin,
Subject
Physics
Biology
Veterinary medicine
Source (journal)
European biophysics journal. - Berlin
Volume/pages
39(2010):8, p. 1129-1142
ISSN
0175-7571
ISI
000279194500003
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Tumor suppressor protein 101F6, a gene product of the 3p21.3 (human) and 9F1 (mouse) chromosomal region, has recently been identified as a member of the cytochrome b561 (Cyt-b561) protein family by sequence homology. The His6-tagged recombinant mouse tumor suppressor Cyt-b561 protein (TSCytb) was recently expressed in yeast and purified, and the ascorbate reducibility was determined. TSCytb is auto-oxidizable and has two distinct heme b centers with redox potentials of ~40 and ~140 mV. Its split α-band in the dithionite-reduced spectrum at both 295 and 77 K is well resolved, and the separation between the two α-peaks is ~7 nm (~222 cm−1). Singular value decomposition analysis of the split α-band in the ascorbate-reduced spectra revealed the presence of two major spectral components, each of them with split α-band but with different peak separations (6 and 8 nm). Similar minor differences in peak separation were obtained when the split α-bands in ascorbate-reduced difference spectra at low (<1 mM) and high (>10 mM) ascorbate concentrations were analysed. According to low-temperature electron paramagnetic resonance (EPR) spectroscopy, the two heme b centers are in the low-spin ferric state with maximum principal g values of 3.61 and 2.96, respectively. These values differ from the ones observed for other members of the Cyt-b561 family. According to resonance Raman spectroscopy, the porphyrin rings are in a relaxed state. The spectroscopic results are only partially in agreement with those obtained earlier for the native chromaffin granule Cyt-b561.
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