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Title: Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 Å resolution
Authors: Ohno, Hiraku
Takeda, Kazuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-4094-6816 (unconfirmed)
Niwa, Satomi
Tsujinaka, Tomotaka
Hanazono, Yuya
Hirano, Yu
Miki, Kunio
Author's alias: 竹田, 一旗
丹羽, 智美
辻中, 智考
花園, 祐矢
平野, 優
三木, 邦夫
Issue Date: 22-May-2017
Publisher: Public Library of Science (PLoS)
Journal title: PLOS ONE
Volume: 12
Issue: 5
Thesis number: e0178183
Abstract: High-potential iron-sulfur protein (HiPIP) is a soluble electron carrier protein of photosynthetic bacteria with an Fe4S4 cluster. Although structural changes accompanying the electron transfer are important for understanding of the functional mechanism, the changes have not been clarified in sufficient detail. We previously reported the high-resolution crystal structures of HiPIP from a thermophilic purple bacterium Thermochromatium tepidum in the reduced state. In order to perform a detailed comparison between the structures in different redox states, the oxidized structure should also be revealed at high resolution. Therefore, in the present study we performed a crystallographic analysis of oxidized HiPIP and a structural comparison with the reduced form at a high resolution of 0.8 Å. The comparison highlighted small but significant contraction in the iron-sulfur cluster. The changes in Fe-S bond lengths were similar to that predicted by theoretical calculation, although some discrepancies were also found. Almost distances between the sulfur atoms of the iron-sulfur cluster and the protein environment are elongated upon the oxidation. Positional changes of hydrogen atoms in the protein environment, such as on the amide-hydrogen of Cys75 in the proximity of the iron-sulfur cluster, were also observed in the accurate analyses. None of the water molecules exhibited significant changes in position or anisotropy of atomic displacement parameter between the two states, while the orientations of some water molecules were different
Rights: © 2017 Ohno et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
URI: http://hdl.handle.net/2433/227729
DOI(Published Version): 10.1371/journal.pone.0178183
PubMed ID: 28542634
Appears in Collections:Journal Articles

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