NDLI: The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli

Please wait, while we are loading the content...

Disruption of zinc and copper interactions with Aβ(1–40) by a non-toxic, isoniazid-derived, hydrazone: a novel biometal homeostasis restoring agent in Alzheimer's disease therapy?

Identification of dopaminergic neurons of the substantia nigra pars compacta as a target of manganese accumulation

Distribution and speciation of bromine in mammalian tissue and fluids by X-ray fluorescence imaging and X-ray absorption spectroscopy

Iron-dependent turnover of IRP-1/c-aconitase in kidney cells

The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli

Copper intoxication inhibits aerobic nucleotide synthesis in Streptococcus pneumoniae

A dual radiolabelling approach for tracking metal complexes: investigating the speciation of copper bis(thiosemicarbazonates) in vitro and in vivo

Common and metal-specific proteomic responses to cadmium and zinc in the metal tolerant ericoid mycorrhizal fungus Oidiodendron maius Zn

In vitro evaluation of the cellular effect of indium tin oxide nanoparticles using the human lung adenocarcinoma A549 cells

Quantitative elemental analysis of bovine ovarian follicles using X-ray fluorescence imaging

Inhibitory effects of NAMI-A-like ruthenium complexes on prion neuropeptide fibril formation

Loss of pdr-1/parkin influences Mn homeostasis through altered ferroportin expression in C. elegans

miRNA plays a role in the antagonistic effect of selenium on arsenic stress in rice seedlings

Protection from neurodegeneration in the 6-hydroxydopamine (6-OHDA) model of Parkinson's with novel 1-hydroxypyridin-2-one metal chelators

An extended siderophore suite from Synechococcus sp. PCC 7002 revealed by LC-ICPMS-ESIMS

In vitro characterization of a novel C,N-cyclometalated benzimidazole Ru(ii) arene complex: stability, intracellular distribution and binding, effects on organic osmolyte homeostasis and induction of apoptosis

Ruthenium complex Λ-WH0402 induces hepatocellular carcinoma LM6 (HCCLM6) cell death by triggering the Beclin-1-dependent autophagy pathway

The effect of gamma-ray irradiation on the Mn(ii) speciation in Deinococcus radiodurans and the potential role of Mn(ii)-orthophosphates

Back cover

Metallomics Vol - 7 Issue - 4

Metallomics Vol - 7 Issue - 3

Metallomics Vol - 7 Issue - 2

The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli

Content Provider	Royal Society of Chemistry (RSC)
Author	Wedd, Anthony G. Xiao, Zhiguang Cortes, Laura
Copyright Year	2015
Abstract	CueO from Escherichia coli is a multicopper oxidase (MCO) involved in copper tolerance under aerobic conditions. It features the four typical copper atoms that act as electron transfer (T1) and dioxygen reduction (T2, T3; trinuclear) sites. In addition, it displays a methionine- and histidine-rich insert that includes a helix that blocks physical access to the T1 site. In crystalline form, the insert provides at least three additional Met-rich Cu(I) binding sites Cu5 (sCu), Cu6 and Cu7 that are proposed to facilitate rapid oxidation of bound Cu(I) to Cu(II) (S. K. Singh, et al., J. Biol. Chem., 2011, 43, 37849–37857). The activities of variants featuring mutations at sites Cu5 (D360M, M355LD360N), Cu6 (M358,362S), Cu7 (M364,368S) and Cu6,7 (M358,362,364,368S) were compared to that of the wild type form using three different air-stable model substrates (2,6-dimethoxyphenol, [CuI(Bca)2]3− and CuICuII-PcoC, a periplasmic Cu(I) binding protein from E. coli). The results demonstrate that the three copper sites play related but distinct roles in CueO oxidase activities. The internal Cu5 site is part of the essential electron transfer pathway connecting surface-exposed sites Cu6 and Cu7 to site T1. Both Cu6 and Cu7 are dominant substrate-docking-oxidation (SDO) sites on the protein surface. However, under physiologically relevant conditions, the SDO function of Cu6 relies largely on an electron transfer pathway via Cu7 to Cu5. These Met-rich sites in CueO provide a robust cuprous oxidase function for control of Cu(I) toxicity.
Starting Page	776
Ending Page	785
Page Count	10
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	7
Issue Number	5
Journal	Metallomics
DOI	10.1039/c5mt00001g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Bca Multicopper oxidase Allotropes of oxygen Syringol Escherichia coli Cellular respiration Methionine Oxidase Singh Biol Copper Protein
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli (2004)

Sequential reconstitution of copper sites in the multicopper oxidase CueO

Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.

Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli.

Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli

Crystal Structures of Multicopper Oxidase CueO Bound to Copper(I) and Silver(I) FUNCTIONAL ROLE OF A METHIONINE-RICH SEQUENCE

Comprehensive Study of the Enzymatic Catalysis of the Electrochemical Oxygen Reduction Reaction (ORR) by Immobilized Copper Efflux Oxidase (CueO) From Escherichia coli

Substrate specificity and copper loading of the manganese-oxidizing multicopper oxidase Mnx from Bacillus sp. PL-12

The multicopper oxidase (CueO) and cell aggregation in Escherichia coli

The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli

Similar Documents

Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli (2004)

Sequential reconstitution of copper sites in the multicopper oxidase CueO

Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.

Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli.

Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli

Crystal Structures of Multicopper Oxidase CueO Bound to Copper(I) and Silver(I) FUNCTIONAL ROLE OF A METHIONINE-RICH SEQUENCE

Comprehensive Study of the Enzymatic Catalysis of the Electrochemical Oxygen Reduction Reaction (ORR) by Immobilized Copper Efflux Oxidase (CueO) From Escherichia coli

Substrate specificity and copper loading of the manganese-oxidizing multicopper oxidase Mnx from Bacillus sp. PL-12

The multicopper oxidase (CueO) and cell aggregation in Escherichia coli

The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli