CuA centers and their biosynthetic models in azurin-Reference-Cited by-同舟云学术

CuA centers and their biosynthetic models in azurin

Published:2010-02-19 Issue:4 Volume:15 Page:461-483
ISSN:0949-8257
Container-title:JBIC Journal of Biological Inorganic Chemistry
language:en
Short-container-title:J Biol Inorg Chem

Author:

Savelieff Masha G.,Lu Yi

Publisher

Springer Science and Business Media LLC

Subject

Inorganic Chemistry,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s00775-010-0625-2.pdf

Reference211 articles.

1. Chan SI, Li PM (1990) Biochemistry 29:1–12

2. Ramirez BE, Malmström BG, Winkler JR, Gray HB (1995) Proc Natl Acad Sci USA 92:11949–11951

3. Ferguson-Miller S, Babcock GT (1996) Chem Rev 96:2889–2907

4. Ostermeier C, Michel H (1997) In: Winkelmann G, Carrano CJ (eds) Transition metals in microbial metabolism, Harwood Academic Publishers, Amsterdam pp 311–328

5. Wikstrom M (2004) Biochim Biophys Acta 1655:241–247

Cited by 44 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Cold-Azurin, a New Antibiofilm Protein Produced by the Antarctic Marine Bacterium Pseudomonas sp. TAE6080;Marine Drugs;2024-01-25

2. A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase;Proceedings of the National Academy of Sciences;2023-10-16

3. Fully Delocalized Mixed‐Valent Cu ^1.5 Cu ^1.5 Complex: Strong Cu‐Cu interaction and Fast Electron Self‐Exchange Rate Despite Large Structural Changes**;Angewandte Chemie International Edition;2023-01-25

4. Fully Delocalized Mixed‐Valent Cu ^1.5 Cu ^1.5 Complex: Strong Cu‐Cu interaction and Fast Electron Self‐Exchange Rate Despite Large Structural Changes**;Angewandte Chemie;2023-01-25

5. Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere;Chemical Reviews;2022-07-11