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...
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2011
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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) |
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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 |
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| _version_ |
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