7qy4 | pdb_00007qy4

As isolated MSOX movie series dataset 5 (2 MGy) of the copper nitrite reductase from Bradyrhizobium sp. ORS 375 (two-domain)

spinqualitylabelsall models 7qy4, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qy4 is a 1 chain structure with sequence from Bradyrhizobium sp. ORS 375. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: CU, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H0SLX7_BRAS3 Publication Abstract from PubMed Many enzymes utilize redox-coupled centers for performing catalysis where these centers are used to control and regulate the transfer of electrons required for catalysis, whose untimely delivery can lead to a state incapable of binding the substrate, i.e., a dead-end enzyme. Copper nitrite reductases (CuNiRs), which catalyze the reduction of nitrite to nitric oxide (NO), have proven to be a good model system for studying these complex processes including proton-coupled electron transfer (ET) and their orchestration for substrate binding/utilization. Recently, a two-domain CuNiR from a Rhizobia species (Br(2D)NiR) has been discovered with a substantially lower enzymatic activity where the catalytic type-2 Cu (T2Cu) site is occupied by two water molecules requiring their displacement for the substrate nitrite to bind. Single crystal spectroscopy combined with MSOX (multiple structures from one crystal) for both the as-isolated and nitrite-soaked crystals clearly demonstrate that inter-Cu ET within the coupled T1Cu-T2Cu redox system is heavily gated. Laser-flash photolysis and optical spectroscopy showed rapid ET from photoexcited NADH to the T1Cu center but little or no inter-Cu ET in the absence of nitrite. Furthermore, incomplete reoxidation of the T1Cu site ( approximately 20% electrons transferred) was observed in the presence of nitrite, consistent with a slow formation of NO species in the serial structures of the MSOX movie obtained from the nitrite-soaked crystal, which is likely to be responsible for the lower activity of this CuNiR. Our approach is of direct relevance for studying redox reactions in a wide range of biological systems including metalloproteins that make up at least 30% of all proteins. Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.,Rose SL, Baba S, Okumura H, Antonyuk SV, Sasaki D, Hedison TM, Shanmugam M, Heyes DJ, Scrutton NS, Kumasaka T, Tosha T, Eady RR, Yamamoto M, Hasnain SS Proc Natl Acad Sci U S A. 2022 Jul 26;119(30):e2205664119. doi:, 10.1073/pnas.2205664119. Epub 2022 Jul 21. PMID:35862453 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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