4XYD

Nitric oxide reductase from Roseobacter denitrificans (RdNOR)

Summary for 4XYD

• Entry DOI: 10.2210/pdb4xyd/pdb
• Descriptor: Nitric-oxide reductase subunit B, NorC-like protein, PROTOPORPHYRIN IX CONTAINING FE, ... (9 entities in total)
• Functional Keywords: nitric oxide reductase, membrane protein, heme copper oxidase superfamily, oxidoreductase
• Biological source: Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)); More
• Total number of polymer chains: 2
• Total formula weight: 70372.32

Authors

Crow, A. (deposition date: 2015-02-02, release date: 2016-05-25, Last modification date: 2024-11-06)

Primary citation

Crow, A.,Matsuda, Y.,Arata, H.,Oubrie, A.
Structure of the Membrane-intrinsic Nitric Oxide Reductase from Roseobacter denitrificans.
Biochemistry, 55:3198-3203, 2016

PubMed Abstract: Membrane-intrinsic nitric oxide reductases (NORs) are key components of bacterial denitrification pathways with a close evolutionary relationship to the cytochrome oxidase (COX) complex found in aerobic respiratory chains. A key distinction between COX and NOR is the identity of the metal directly opposite heme b3 within the active site. In NOR, this metal is iron (FeB), whereas in COX, it is copper (CuB). The purified NOR of Roseobacter denitrificans contains copper and has modest oxidase activity, raising the possibility that a COX-like active site might have independently arisen within the context of a NOR-like protein scaffold. Here we present the crystal structure of the Roseobacter denitrificans NorBC complex and anomalous scattering experiments probing the identity of each metal center. Our results refute the hypothesis that copper occupies the active site and instead reveal a new metal center in the small subunit not seen in any other NOR or COX.

PubMed: 27185533
DOI: 10.1021/acs.biochem.6b00332

Experimental method

X-RAY DIFFRACTION (2.85 Å)