6Y7E

Pseudomonas stutzeri nitrous oxide reductase mutant, H494A

6Y7E の概要

• エントリーDOI: 10.2210/pdb6y7e/pdb
• 分子名称: Nitrous-oxide reductase, FORMIC ACID, ZINC ION, ... (10 entities in total)
• 機能のキーワード: periplasmic copper-binding protein, oxidoreductase
• 由来する生物種: Pseudomonas stutzeri
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 145261.25

構造登録者

Zhang, L.,Kroneck, P.M.H.,Einsle, O. (登録日: 2020-02-28, 公開日: 2021-01-27, 最終更新日: 2024-01-24)

主引用文献

Zhang, L.,Bill, E.,Kroneck, P.M.H.,Einsle, O.
A [3Cu:2S] cluster provides insight into the assembly and function of the Cu Z site of nitrous oxide reductase.
Chem Sci, 12:3239-3244, 2021

PubMed Abstract: Nitrous oxide reductase (NOR) is the only known enzyme reducing environmentally critical nitrous oxide (NO) to dinitrogen (N) as the final step of bacterial denitrification. The assembly process of its unique catalytic [4Cu:2S] cluster Cu remains scarcely understood. Here we report on a mutagenesis study of all seven histidine ligands coordinating this copper center, followed by spectroscopic and structural characterization and based on an established, functional expression system for NOR in . While no copper ion was found in the Cu binding site of variants H129A, H130A, H178A, H326A, H433A and H494A, the H382A variant carried a catalytically inactive [3Cu:2S] center, in which one sulfur ligand, S, had relocated to form a weak hydrogen bond to the sidechain of the nearby lysine residue K454. This link provides sufficient stability to avoid the loss of the sulfide anion. The UV-vis spectra of this cluster are strikingly similar to those of the active enzyme, implying that the flexibility of S may have been observed before, but not recognized. The sulfide shift changes the metal coordination in Cu and is thus of high mechanistic interest.

PubMed: 34164092
DOI: 10.1039/d0sc05204c

実験手法

X-RAY DIFFRACTION (1.6 Å)