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Horse heart cytochrome c entrapped into the hydrated liquid-crystalline phases of phytantriol: X-ray diffraction and Raman spectroscopic characterization

Misiunas, Audrius; Niaura, Gediminas; Barauskas, Justas; Meskys, Rolandas; Rutkiene, Rasa; Razumas, Valdemaras and Nylander, Tommy LU (2012) In Journal of Colloid and Interface Science 378. p.232-240
Abstract
Small angle X-ray diffraction (SAXD), resonance Raman (RR) spectroscopy with 413 nm excitation, and non-resonance Raman technique with 785 nm excitation were used to probe the influence of entrapped cytochrome c (Cyt c) on the structure of hydrated phytantriol (Phyt) liquid-crystalline phases as well as conformational changes of heme group and secondary structure of the protein. SAXD measurements indicated that incorporation of Cyt c affects both nanostructure dimensions and type of liquid-crystalline phases of hydrated Phyt. The unit cell dimensions decrease with increasing Cyt c concentration for all phases. In addition, protein perturbs the nanostructure of Q(230) and Q(224) liquid-crystalline phases of hydrated Phyt to such an extent... (More)
Small angle X-ray diffraction (SAXD), resonance Raman (RR) spectroscopy with 413 nm excitation, and non-resonance Raman technique with 785 nm excitation were used to probe the influence of entrapped cytochrome c (Cyt c) on the structure of hydrated phytantriol (Phyt) liquid-crystalline phases as well as conformational changes of heme group and secondary structure of the protein. SAXD measurements indicated that incorporation of Cyt c affects both nanostructure dimensions and type of liquid-crystalline phases of hydrated Phyt. The unit cell dimensions decrease with increasing Cyt c concentration for all phases. In addition, protein perturbs the nanostructure of Q(230) and Q(224) liquid-crystalline phases of hydrated Phyt to such an extent that they transform into the Q(229) phase with the Im3m space group. RR data revealed that entrapment of oxidized Cyt c into the Q(230) phase at 1 wt.% content results in near complete reduction of central iron ion of the heme group, while its low-spin state and six-ligand coordination configuration are preserved. Based on the analysis of heme out-of-plane folding vibration near 568 cm(-1) (gamma(21)) and nu(48) mode at 633 cm(-1), it was demonstrated that the protein matrix tension on the heme group is relaxed upon incorporation of protein into Q(230) phase. Non-resonant Raman bands of difference spectra showed the preservation of alpha-helix secondary structure of Cyt c in the liquid-crystalline phase at relatively high (5 wt.%) content. The Cyt c induced spectroscopic changes of Phyt bands were found to be similar as decrease in temperature. (C) 2012 Elsevier Inc. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Phytantriol, Cytochrome c, SAXD, Resonance Raman spectroscopy, Liquid-crystalline phases
in
Journal of Colloid and Interface Science
volume
378
pages
232 - 240
publisher
Elsevier
external identifiers
  • wos:000305165500029
  • scopus:84861571774
ISSN
1095-7103
DOI
10.1016/j.jcis.2012.04.002
language
English
LU publication?
yes
id
abc06503-6f89-420a-b5ab-b85780360c04 (old id 2891017)
date added to LUP
2012-07-25 16:55:15
date last changed
2017-05-21 03:17:18
@article{abc06503-6f89-420a-b5ab-b85780360c04,
  abstract     = {Small angle X-ray diffraction (SAXD), resonance Raman (RR) spectroscopy with 413 nm excitation, and non-resonance Raman technique with 785 nm excitation were used to probe the influence of entrapped cytochrome c (Cyt c) on the structure of hydrated phytantriol (Phyt) liquid-crystalline phases as well as conformational changes of heme group and secondary structure of the protein. SAXD measurements indicated that incorporation of Cyt c affects both nanostructure dimensions and type of liquid-crystalline phases of hydrated Phyt. The unit cell dimensions decrease with increasing Cyt c concentration for all phases. In addition, protein perturbs the nanostructure of Q(230) and Q(224) liquid-crystalline phases of hydrated Phyt to such an extent that they transform into the Q(229) phase with the Im3m space group. RR data revealed that entrapment of oxidized Cyt c into the Q(230) phase at 1 wt.% content results in near complete reduction of central iron ion of the heme group, while its low-spin state and six-ligand coordination configuration are preserved. Based on the analysis of heme out-of-plane folding vibration near 568 cm(-1) (gamma(21)) and nu(48) mode at 633 cm(-1), it was demonstrated that the protein matrix tension on the heme group is relaxed upon incorporation of protein into Q(230) phase. Non-resonant Raman bands of difference spectra showed the preservation of alpha-helix secondary structure of Cyt c in the liquid-crystalline phase at relatively high (5 wt.%) content. The Cyt c induced spectroscopic changes of Phyt bands were found to be similar as decrease in temperature. (C) 2012 Elsevier Inc. All rights reserved.},
  author       = {Misiunas, Audrius and Niaura, Gediminas and Barauskas, Justas and Meskys, Rolandas and Rutkiene, Rasa and Razumas, Valdemaras and Nylander, Tommy},
  issn         = {1095-7103},
  keyword      = {Phytantriol,Cytochrome c,SAXD,Resonance Raman spectroscopy,Liquid-crystalline phases},
  language     = {eng},
  pages        = {232--240},
  publisher    = {Elsevier},
  series       = {Journal of Colloid and Interface Science},
  title        = {Horse heart cytochrome c entrapped into the hydrated liquid-crystalline phases of phytantriol: X-ray diffraction and Raman spectroscopic characterization},
  url          = {http://dx.doi.org/10.1016/j.jcis.2012.04.002},
  volume       = {378},
  year         = {2012},
}