Horse heart cytochrome c entrapped into the hydrated liquid-crystalline phases of phytantriol: X-ray diffraction and Raman spectroscopic characterization
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2891017
- author
- Misiunas, Audrius ; Niaura, Gediminas ; Barauskas, Justas ; Meskys, Rolandas ; Rutkiene, Rasa ; Razumas, Valdemaras and Nylander, Tommy LU
- organization
- publishing date
- 2012
- 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
- pmid:22546244
- 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
- 2016-04-01 10:41:44
- date last changed
- 2023-08-31 09:01:39
@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}},
keywords = {{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}},
doi = {{10.1016/j.jcis.2012.04.002}},
volume = {{378}},
year = {{2012}},
}