The unexpected structural role of glutamate synthase [4Fe–4S]+1,+2 clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme β subunit-Reference-Cited by-同舟云学术

The unexpected structural role of glutamate synthase [4Fe–4S]+1,+2 clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme β subunit

Published:2005-04 Issue:2 Volume:436 Page:355-366
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Agnelli Paola,Dossena Laura,Colombi Paolo,Mulazzi Sara,Morandi Paola,Tedeschi Gabriella,Negri Armando,Curti Bruno,Vanoni Maria A.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

1. Glutamate synthase: a complex iron-sulfur flavoprotein

2. Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate

3. Structure–function studies on the iron–sulfur flavoenzyme glutamate synthase: an unexpectedly complex self-regulated enzyme

4. Structure–function studies on the complex iron–sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation

5. Cross-Talk and Ammonia Channeling between Active Centers in the Unexpected Domain Arrangement of Glutamate Synthase

Cited by 9 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. Iron-sulfur flavoenzymes: the added value of making the most ancient redox cofactors and the versatile flavins work together;Open Biology;2021-05

2. Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies;Journal of Molecular Biology;2019-11

3. The l-Thr Kinase/l-Thr-Phosphate Decarboxylase (CobD) Enzyme from Methanosarcina mazei Gö1 Contains Metallocenters Needed for Optimal Activity;Biochemistry;2019-07-03

4. Glutamate synthase: A case-study for in silico drug screening on a complex iron–sulfur flavoenzyme?;Gene;2015-06

5. Tunnels and Intermediates in the Glutamine-Dependent Amidotransferases;Comprehensive Natural Products II;2010