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Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17‐16 laccase influence enzymatic prope...

Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17‐16 laccase influence enzymatic prope...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_8bc3496b1b2b4cb39dd55626e9998372

Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17‐16 laccase influence enzymatic properties

About this item

Full title

Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17‐16 laccase influence enzymatic properties

Publisher

England: John Wiley & Sons, Inc

Journal title

FEBS open bio, 2019-05, Vol.9 (5), p.986-995

Language

English

Formats

Publication information

Publisher

England: John Wiley & Sons, Inc

More information

Scope and Contents

Contents

Laccase is a multi‐copper oxidase which oxidizes substrate at the type 1 copper site, simultaneously coupling the reduction of dioxygen to water at the trinuclear copper center. In this study, we used site‐directed mutagenesis to study the effect of axial bonds between the metal and amino acid residue side chains in lacTT. Our kinetic and spectral...

Alternative Titles

Full title

Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17‐16 laccase influence enzymatic properties

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_8bc3496b1b2b4cb39dd55626e9998372

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_8bc3496b1b2b4cb39dd55626e9998372

Other Identifiers

ISSN

2211-5463

E-ISSN

2211-5463

DOI

10.1002/2211-5463.12633

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