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An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures. | LitMetric

An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.

Sci Adv

Molecular Biophysics Group, Life Sciences Building and Institute of Systems, Molecular and Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, UK.

Published: January 2021

Copper-containing nitrite reductases (CuNiRs), encoded by gene, are found in all kingdoms of life with only 5% of CuNiR denitrifiers having two or more copies of Recently, we have identified two copies of genes in several α-proteobacteria of the order Rhizobiales including sp. ORS 375, encoding a four-domain heme-CuNiR and the usual two-domain CuNiR ( NiR). Compared with two of the best-studied two-domain CuNiRs represented by the blue (NiR) and green (NiR) subclasses, NiR, a blue CuNiR, shows a substantially lower catalytic efficiency despite a sequence identity of ~70%. Advanced synchrotron radiation and x-ray free-electron laser are used to obtain the most accurate (atomic resolution with unrestrained SHELX refinement) and damage-free (free from radiation-induced chemistry) structures, in as-isolated, substrate-bound, and product-bound states. This combination has shed light on the protonation states of essential catalytic residues, additional reaction intermediates, and how catalytic efficiency is modulated.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7775769PMC
http://dx.doi.org/10.1126/sciadv.abd8523DOI Listing

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