Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.

To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Wenxian Lan, Zhonghua Wang, Zhongzheng Yang, Jing Zhu, Tianlei Ying, Xianwang Jiang, Xu Zhang, Houming Wu, Maili Liu, Xiangshi Tan, Chunyang Cao, Zhong-Xian Huang
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2011
Materias:
R
Q
Acceso en línea:https://doaj.org/article/c3757a2a4ad44e8c9c0077fd8210a03c
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:c3757a2a4ad44e8c9c0077fd8210a03c
record_format dspace
spelling oai:doaj.org-article:c3757a2a4ad44e8c9c0077fd8210a03c2021-11-18T07:34:45ZConformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.1932-620310.1371/journal.pone.0027219https://doaj.org/article/c3757a2a4ad44e8c9c0077fd8210a03c2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22087268/?tool=EBIhttps://doaj.org/toc/1932-6203To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance Raman spectroscopy. To further probe the functional importance of Pro71 in oxidation state dependent conformational changes occurred in cyt c, the solution structures of P71H mutant in both oxidation states were determined. The structures indicate that the half molecule of cyt c (aa 50-102) presents a kind of "zigzag riveting ruler" structure, residues at certain positions of this region such as Pro71, Lys73 can move a big distance by altering the tertiary structure while maintaining the secondary structures. This finding provides a molecular insight into conformational toggling in different oxidation states of cyt c that is principle significance to its biological functions in electron transfer and apoptosis. Structural analysis also reveals that Pro71 functions as a key hydrophobic patch in the folding of the polypeptide of the region (aa 50-102), to prevent heme pocket from the solvent.Wenxian LanZhonghua WangZhongzheng YangJing ZhuTianlei YingXianwang JiangXu ZhangHouming WuMaili LiuXiangshi TanChunyang CaoZhong-Xian HuangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 11, p e27219 (2011)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Wenxian Lan
Zhonghua Wang
Zhongzheng Yang
Jing Zhu
Tianlei Ying
Xianwang Jiang
Xu Zhang
Houming Wu
Maili Liu
Xiangshi Tan
Chunyang Cao
Zhong-Xian Huang
Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
description To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance Raman spectroscopy. To further probe the functional importance of Pro71 in oxidation state dependent conformational changes occurred in cyt c, the solution structures of P71H mutant in both oxidation states were determined. The structures indicate that the half molecule of cyt c (aa 50-102) presents a kind of "zigzag riveting ruler" structure, residues at certain positions of this region such as Pro71, Lys73 can move a big distance by altering the tertiary structure while maintaining the secondary structures. This finding provides a molecular insight into conformational toggling in different oxidation states of cyt c that is principle significance to its biological functions in electron transfer and apoptosis. Structural analysis also reveals that Pro71 functions as a key hydrophobic patch in the folding of the polypeptide of the region (aa 50-102), to prevent heme pocket from the solvent.
format article
author Wenxian Lan
Zhonghua Wang
Zhongzheng Yang
Jing Zhu
Tianlei Ying
Xianwang Jiang
Xu Zhang
Houming Wu
Maili Liu
Xiangshi Tan
Chunyang Cao
Zhong-Xian Huang
author_facet Wenxian Lan
Zhonghua Wang
Zhongzheng Yang
Jing Zhu
Tianlei Ying
Xianwang Jiang
Xu Zhang
Houming Wu
Maili Liu
Xiangshi Tan
Chunyang Cao
Zhong-Xian Huang
author_sort Wenxian Lan
title Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
title_short Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
title_full Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
title_fullStr Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
title_full_unstemmed Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.
title_sort conformational toggling of yeast iso-1-cytochrome c in the oxidized and reduced states.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doaj.org/article/c3757a2a4ad44e8c9c0077fd8210a03c
work_keys_str_mv AT wenxianlan conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT zhonghuawang conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT zhongzhengyang conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT jingzhu conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT tianleiying conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT xianwangjiang conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT xuzhang conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT houmingwu conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT maililiu conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT xiangshitan conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT chunyangcao conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
AT zhongxianhuang conformationaltogglingofyeastiso1cytochromecintheoxidizedandreducedstates
_version_ 1718423249251991552