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Article

Histidine substitution in the most flexible fragments of firefly luciferase modifies its thermal stability.

Archives of biochemistry and biophysics - 1 Sept 2017

Rahban Mahdie, Salehi Najmeh, Saboury Ali Akbar, Hosseinkhani Saman, Karimi-Jafari Mohammad Hossein, Firouzi Rohoullah, Rezaei-Ghaleh Nasrollah, Moosavi-Movahedi Ali Akbar

Abstract excerpt

Molecular dynamics (MD) at two temperatures of 300 and 340 K identified two histidine residues, His461 and His489, in the most flexible regions of firefly luciferase, a light emitting enzyme. We therefore designed four protein mutants H461D, H489K, H489D and H489M to investigate their enzyme kinetic and thermodynamic stability changes. Substitution of His461 by aspartate (H461D) decreased ATP binding affinity,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 28711358
DOI: 10.1016/j.abb.2017.07.003

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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