Detalhe da pesquisa
1.
Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.
Proc Natl Acad Sci U S A
; 119(30): e2205664119, 2022 07 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-35862453
2.
Structures of protein-protein complexes involved in electron transfer.
Nature
; 496(7443): 123-6, 2013 Apr 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-23535590
3.
Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy.
Acta Crystallogr D Biol Crystallogr
; 70(Pt 5): 1289-96, 2014 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-24816098
4.
Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.
Proc Natl Acad Sci U S A
; 108(38): 15780-5, 2011 Sep 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-21900609
5.
Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii.
Biochem J
; 444(2): 219-26, 2012 Jun 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-22414182
6.
A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.
Nat Commun
; 14(1): 3416, 2023 06 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-37296134
7.
A distal pocket Leu residue inhibits the binding of O2 and NO at the distal heme site of cytochrome c'.
J Am Chem Soc
; 134(3): 1461-3, 2012 Jan 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-22239663
8.
Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase.
Biochemistry
; 50(19): 4121-31, 2011 May 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-21469743
9.
Electron transfer and half-reactivity in nitrogenase.
Biochem Soc Trans
; 39(1): 201-6, 2011 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-21265773
10.
Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction.
FEBS J
; 288(1): 262-280, 2021 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-32255260
11.
An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.
Sci Adv
; 7(1)2021 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-33523860
12.
Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases.
J Biol Chem
; 284(38): 25973-83, 2009 Sep 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-19586913
13.
Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis.
Chem Sci
; 11(46): 12485-12492, 2020 Oct 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-34094452
14.
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes.
IUCrJ
; 7(Pt 3): 557-565, 2020 May 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-32431838
15.
Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography.
IUCrJ
; 6(Pt 4): 761-772, 2019 Jul 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-31316819
16.
Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
ACS Catal
; 9(7): 6087-6099, 2019 Jul 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-32051772
17.
Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants.
Biochemistry
; 47(51): 13547-53, 2008 Dec 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-19053252
18.
Identification of a tyrosine switch in copper-haem nitrite reductases.
IUCrJ
; 5(Pt 4): 510-518, 2018 Jul 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-30002851
19.
An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase.
IUCrJ
; 5(Pt 1): 22-31, 2018 Jan 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-29354268
20.
Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.
IUCrJ
; 5(Pt 3): 283-292, 2018 May 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-29755744