Folding dynamics of phenylalanine hydroxylase depends on the enzyme’s metallation state: the native metal, iron, protects against aggregate intermediates-Reference-Cited by-同舟云学术

Folding dynamics of phenylalanine hydroxylase depends on the enzyme’s metallation state: the native metal, iron, protects against aggregate intermediates

Published:2011-06-07 Issue:8 Volume:40 Page:959-968
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

Loaiza Aristobulo,Ronau Judith A.,Ribbe Alexander,Stanciu Lia,Burgner John W.,Paul Lake N.,Abu-Omar Mahdi M.

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/s00249-011-0711-6.pdf

Reference45 articles.

1. Abu-Omar MM, Loaiza A, Hontzeas N (2005) Reaction mechanisms of mononuclear non-heme iron oxygenases. Chem Rev 105:2227–2252

2. Bjorgo E, Knappskog PM, Martinez A, Stevens RC, Flatmark T (1998) Partial characterization of three-dimensional structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria. Eur J Biochem 257:1–10

3. Brown PH, Schuck P (2006) Macromolecular size and shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys J 90:4651–4661

4. Carr RT, Balasubramanian S, Hawkins PCD, Benkovic SJ (1995) Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Biochemistry 34:7525–7532

5. Chen D, Frey P (1998) Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation. J Biol Chem 273:25594–25601

Cited by 3 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. The chaperone role of the pyridoxal 5′-phosphate and its implications for rare diseases involving B6-dependent enzymes;Clinical Biochemistry;2014-02

2. Monitoring the Biomolecular Interactions and the Activity of Zn-Containing Enzymes Involved in Conformational Diseases;Metal-Containing Enzymes;2014

3. Metal complexes and metalloproteases: targeting conformational diseases;Metallomics;2014