Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR

Cytochrome c (cyt c) is an important multifunctional protein. In mitochondria, it acts as a carrier for electron transporting. In cytoplasm, it may act as an apoptotic initiator to initiate the apoptotic process. Whether and how a complex cytoplasmic environment affects its conformation has not been...

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Main Authors: ZHAN Jianhua, 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China, ZHU Qinjun, JIANG Bin, 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China, LIU Maili
Format: Article
Language:zho
Published: Science Press 2023-03-01
Series:Chinese Journal of Magnetic Resonance
Subjects:
Online Access:http://121.43.60.238/bpxzz/article/2023/1000-4556/1000-4556-40-1-22.shtml
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author ZHAN Jianhua
1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China
ZHU Qinjun
JIANG Bin
1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China
LIU Maili
author_facet ZHAN Jianhua
1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China
ZHU Qinjun
JIANG Bin
1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China
LIU Maili
author_sort ZHAN Jianhua
collection DOAJ
description Cytochrome c (cyt c) is an important multifunctional protein. In mitochondria, it acts as a carrier for electron transporting. In cytoplasm, it may act as an apoptotic initiator to initiate the apoptotic process. Whether and how a complex cytoplasmic environment affects its conformation has not been confirmed yet. In this study, the conformational changes of wild type saccharomyces cerevisiae iso-1 cyt c in yeast cell homogenate were tracked by methyl-based nuclear magnetic resonance (NMR) technique. At least four different oxidative conformations and one reduced conformation of cyt c were identified in cell homogenate. And over time, the transitions among different conformations of cyt c were observed. The results indicate that the conformation of cyt c changes with environment, which may be closely related to resistance to oxidative stress.
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spelling doaj.art-5567bfd7087645148bbd1102da86fca92023-04-07T01:41:42ZzhoScience PressChinese Journal of Magnetic Resonance1000-45562023-03-01401222910.11938/cjmr20222985Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMRZHAN Jianhua01. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China1 ZHU Qinjun2JIANG Bin31. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China4LIU Maili51. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, ChinaCytochrome c (cyt c) is an important multifunctional protein. In mitochondria, it acts as a carrier for electron transporting. In cytoplasm, it may act as an apoptotic initiator to initiate the apoptotic process. Whether and how a complex cytoplasmic environment affects its conformation has not been confirmed yet. In this study, the conformational changes of wild type saccharomyces cerevisiae iso-1 cyt c in yeast cell homogenate were tracked by methyl-based nuclear magnetic resonance (NMR) technique. At least four different oxidative conformations and one reduced conformation of cyt c were identified in cell homogenate. And over time, the transitions among different conformations of cyt c were observed. The results indicate that the conformation of cyt c changes with environment, which may be closely related to resistance to oxidative stress.http://121.43.60.238/bpxzz/article/2023/1000-4556/1000-4556-40-1-22.shtmlnuclear magnetic resonance (nmr)conformational changemethylcytochrome c
spellingShingle ZHAN Jianhua
1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China
ZHU Qinjun
JIANG Bin
1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China
LIU Maili
Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR
Chinese Journal of Magnetic Resonance
nuclear magnetic resonance (nmr)
conformational change
methyl
cytochrome c
title Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR
title_full Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR
title_fullStr Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR
title_full_unstemmed Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR
title_short Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR
title_sort track the conformational change of unlabeled yeast cytochrome c in cell homogenate using nmr
topic nuclear magnetic resonance (nmr)
conformational change
methyl
cytochrome c
url http://121.43.60.238/bpxzz/article/2023/1000-4556/1000-4556-40-1-22.shtml
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