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Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography

Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_1517770113

Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography

About this item

Full title

Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2016-03, Vol.113 (11), p.2928-2933

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Proton-coupled electron transfer (PCET), a ubiquitous phenomenon in biological systems, plays an essential role in copper nitrite reductase (CuNiR), the key metalloenzyme in microbial denitrification of the global nitrogen cycle. Analyses of the nitrite reduction mechanism in CuNiR with conventional synchrotron radiation crystallography (SRX) have...

Alternative Titles

Full title

Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_primary_10_1073_pnas_1517770113

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_1517770113

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1517770113

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