.png){kind=icon}
返回
Type-zero copper proteins
.png){kind=icon}
OA
AI
DOI：10.1038/NCHEM.412.png)
.png){kind=icon}
.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Many proteins contain copper in a range of coordination environments, where it has various biological roles, such as transferring electrons or activating dioxygen. These copper sites can be classified by their function or spectroscopic properties. Those with a single copper atom are either type 1, with an intense absorption band near 600 nm, or type 2, with weak absorption in the visible region. We have built a novel copper(II) binding site within structurally modified Pseudomonas aeruginosa azurins that does not resemble either existing type, which we therefore call 'type zero'. X-ray crystallographic analysis shows that these sites adopt distorted tetrahedral geometries, with an unusually short Cu-O (G45 carbonyl) bond. Relatively weak absorption near 800 nm and narrow parallel hyperfine splittings in electron paramagnetic resonance spectra are the spectroscopic signatures of type zero copper. Cyclic voltammetric experiments demonstrate that the electron transfer reactivities of type-zero azurins are enhanced relative to that of the corresponding type 2 (C112D) protein.
Keyword:
ELECTRON-TRANSFER
CRYSTAL-STRUCTURE
ACTIVE-SITE
BLUE
REDUCTION
AZURIN
CUEO
OXIDASE
O-2
CHEMISTRY
AI总结
对已上传原文的论文进行重点信息的提取，主要内容包括：简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
IF:
20.2
论文数:
4.4K
被引数:
4.8W
机构
引用论文
Evidence of organic structures in Ediacara-type fossils and associated microbial mats.png)
Geology
GeologyIF0
PREAI
分享收藏分享收藏High-Potential C112D/M121X (X = M, E H, L) Pseudomonas aeruginosa AzurinsINORGANIC CHEMISTRYOAAI
INORGANIC CHEMISTRYIF4.7
OAAI分享收藏
查看更多内容