Structure of Escherichia coli Flavodiiron Nitric Oxide Reductase
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- 作者：Cé ; lia V. Romã ; o1 ; Joã ; o B. Vicente1 ; Patrí ; cia T. Borges1 ; Bruno L. Victor1 ; 3 ; Pedro Lamosa1 ; Elí ; sio Silva1 ; Luí ; s Pereira1 ; Tiago M. Bandeiras1 ; 2 ; Clá ; udio M. Soares1 ; Maria A. Carrondo1 ; David Turner1 ; Miguel Teixeira1 ; miguel@itqb.unl.pt" class="auth_mail" title="E-mail the corresponding author ; Carlos Frazã ; o1 ; frazao@itqb.unl.pt" class="auth_mail" title="E-mail the corresponding author
- 关键词：NO ; nitric oxide ; Hmp ; flavohaemoglobin ; FlRd ; flavorubredoxin ; FDP ; flavodiiron protein ; FMN ; flavin mononucleotide ; Rd ; rubredoxin ; MD ; molecular dynamics ; SAXS ; small-angle X-ray scattering ; a.u. ; asymmetric unit ; SAS ; solvent-accessible surface ; a.d.p. ; atomic displacement parameter ; μ-OHˉ ; μ-hydroxo ; PEG ; polyethylene glycol ; ESRF ; European Synchrotron Research Facility ; DLS ; Diamond Light Source ; TLS ; translation ; libration ; and screw ; NOESY ; Nuclear Overhauser enhancement spectroscopy ; TO
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：20 November 2016
- 年：2016
- 卷：428
- 期：23
- 页码：4686-4707
- 全文大小：4106 K
文摘
Crystal structure of the NO selective Escherichia coli flavodiiron protein
Oxidized and reduced protein crystals reveal structural differences at the diiron site.
Protein tunnels for substrates/products were identified.
Chain of aromatic residues connects the diiron site to the protein surface.