📣 Help Shape the Future of UKRI's Gateway to Research (GtR)

We're improving UKRI's Gateway to Research and are seeking your input! If you would be interested in being interviewed about the improvements we're making and to have your say about how we can make GtR more user-friendly, impactful, and effective for the Research and Innovation community, please email gateway@ukri.org.

Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes. (2020)

First Author: Sasaki D

Attributed to: Why does Nature use modular enzyme architectures for biological catalysis? funded by BBSRC

Abstract

No abstract provided

Bibliographic Information

Digital Object Identifier: http://dx.doi.org/10.1107/s2052252520005230

PubMed Identifier: 32431838

Publication URI: http://europepmc.org/abstract/MED/32431838

Type: Journal Article/Review

Volume: 7

Parent Publication: IUCrJ

Issue: Pt 3

ISSN: 2052-2525