• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

Contact shifts and magnetic susceptibilities in iron-sulfur proteins as determined from nuclear magnetic resonance spectra.

作者信息

Phillips W D, Poe M

出版信息

Methods Enzymol. 1972;24:304-17. doi: 10.1016/0076-6879(72)24077-0.

DOI:10.1016/0076-6879(72)24077-0
PMID:4670195
Abstract
摘要

相似文献

1
Contact shifts and magnetic susceptibilities in iron-sulfur proteins as determined from nuclear magnetic resonance spectra.
Methods Enzymol. 1972;24:304-17. doi: 10.1016/0076-6879(72)24077-0.
2
Low-temperature magnetic circular dichroism spectra and magnetisation curves of 4Fe clusters in iron-sulphur proteins from Chromatium and Clostridium pasteurianum.来自嗜硫色杆菌和巴氏梭菌的铁硫蛋白中4Fe簇的低温磁圆二色光谱和磁化曲线。
Biochim Biophys Acta. 1981 Feb 27;667(2):433-51. doi: 10.1016/0005-2795(81)90209-9.
3
The iron electron-nuclear double resonance (ENDOR) of 4-Fe clusters in iron-sulfur proteins from Chromatium and Clostridium pasteurianum.来自嗜硫色杆菌和巴氏梭菌的铁硫蛋白中4-铁簇的铁电子-核双共振(ENDOR)
Biochim Biophys Acta. 1975 Jan 31;376(1):63-71. doi: 10.1016/0005-2728(75)90204-2.
4
Cluster characterization in iron-sulfur proteins by magnetic circular dichroism.通过磁圆二色性对铁硫蛋白进行簇表征。
Proc Natl Acad Sci U S A. 1978 Nov;75(11):5273-5. doi: 10.1073/pnas.75.11.5273.
5
Circular dichroism and magnetic circular dichroism of iron-sulfur proteins.铁硫蛋白的圆二色性和磁圆二色性
Biochemistry. 1978 Oct 31;17(22):4770-8. doi: 10.1021/bi00615a026.
6
Synthetic analogs of the active sites of iron-sulfur proteins. 8. Some electronic properties of (Fe4S4(SR)4)3-, analogs of reduced bacterial ferredoxins.
Biochem Biophys Res Commun. 1974 Jun 18;58(4):974-82. doi: 10.1016/s0006-291x(74)80239-1.
7
The use of 13C nuclear magnetic resonance of aromatic amino acid residues to determine the midpoint oxidation-reduction potential of each iron-sulfur cluster of Clostridium acidi-urici and Clostridium pasteurianum ferredoxins.利用芳香族氨基酸残基的13C核磁共振来测定尿酸梭菌和巴氏梭菌铁氧化还原蛋白中每个铁硫簇的中点氧化还原电位。
J Biol Chem. 1975 Mar 25;250(6):2062-72.
8
Identification of iron--sulfur clusters in proteins.
Methods Enzymol. 1978;53:268-74. doi: 10.1016/s0076-6879(78)53032-2.
9
Determination of oxidation-reduction potentials by spectropolarimetric titration: application to several iron-sulfur proteins.通过分光偏振滴定法测定氧化还原电位:应用于几种铁硫蛋白。
Arch Biochem Biophys. 1974 May;162(1):301-9. doi: 10.1016/0003-9861(74)90129-5.
10
X-ray photoelectron spectra of iron-sulphur proteins.铁硫蛋白的X射线光电子能谱
Biochem J. 1975 Aug;149(2):471-4. doi: 10.1042/bj1490471.

引用本文的文献

1
Role of the iron axial ligands of heme carrier HasA in heme uptake and release.亚铁轴向配体在血红素载体 HasA 摄取和释放中的作用。
J Biol Chem. 2012 Aug 3;287(32):26932-43. doi: 10.1074/jbc.M112.366385. Epub 2012 Jun 14.
2
NMR reveals pathway for ferric mineral precursors to the central cavity of ferritin.核磁共振揭示了铁矿物前体进入铁蛋白中心腔的途径。
Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):545-50. doi: 10.1073/pnas.0908082106. Epub 2009 Dec 16.
3
Nuclear magnetic resonance characterization of a paramagnetic DNA-drug complex with high spin cobalt; assignment of the 1H and 31P NMR spectra, and determination of electronic, spectroscopic and molecular properties.
具有高自旋钴的顺磁性DNA-药物复合物的核磁共振表征;1H和31P NMR谱的归属以及电子、光谱和分子性质的测定。
J Biomol NMR. 1998 Aug;12(2):243-57. doi: 10.1023/a:1008289724077.
4
Fluorine-19 chemical shifts as structural probes of metal-sulfur clusters and the cofactor of nitrogenase.氟-19化学位移作为金属硫簇和固氮酶辅因子的结构探针。
Proc Natl Acad Sci U S A. 1982 Nov;79(22):7056-60. doi: 10.1073/pnas.79.22.7056.
5
Proton magnetic resonance and magnetic susceptibility characterization of ferredoxin I from Bacillus polymyxa.多粘芽孢杆菌铁氧化还原蛋白I的质子磁共振和磁化率表征
Proc Natl Acad Sci U S A. 1974 Jan;71(1):140-3. doi: 10.1073/pnas.71.1.140.