Horrell, S and Kekilli, D and Strange, RW and Hough, MA (2017) Recent structural insights into the function of copper nitrite reductases. Metallomics, 9 (11). pp. 1470-1482. DOI https://doi.org/10.1039/c7mt00146k
Horrell, S and Kekilli, D and Strange, RW and Hough, MA (2017) Recent structural insights into the function of copper nitrite reductases. Metallomics, 9 (11). pp. 1470-1482. DOI https://doi.org/10.1039/c7mt00146k
Horrell, S and Kekilli, D and Strange, RW and Hough, MA (2017) Recent structural insights into the function of copper nitrite reductases. Metallomics, 9 (11). pp. 1470-1482. DOI https://doi.org/10.1039/c7mt00146k
Abstract
Copper nitrite reductases (CuNiR) carry out the first committed step of the denitrification pathway of the global nitrogen cycle, the reduction of nitrite (NO2(-)) to nitric oxide (NO). As such, they are of major agronomic and environmental importance. CuNiRs occur primarily in denitrifying soil bacteria which carry out the overall reduction of nitrate to dinitrogen. In this article, we review the insights gained into copper nitrite reductase (CuNiR) function from three dimensional structures. We particularly focus on developments over the last decade, including insights from serial femtosecond crystallography using X-ray free electron lasers (XFELs) and from the recently discovered 3-domain CuNiRs.
Item Type: | Article |
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Uncontrolled Keywords: | Nitrites; Copper; Nitric Oxide; Nitrite Reductases; Bacterial Proteins; Crystallography, X-Ray; Protein Binding; Electron Transport; Models, Molecular; Protein Domains |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 04 Aug 2017 15:45 |
Last Modified: | 30 Oct 2024 17:08 |
URI: | http://repository.essex.ac.uk/id/eprint/20178 |
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Licence: Creative Commons: Attribution 3.0