Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.
Tobias M HedisonAndreea I IorguDonato CalabreseDerren J HeyesMuralidharan ShanmugamNigel S ScruttonPublished in: The journal of physical chemistry letters (2022)
Copper nitrite reductases (CuNiRs) catalyze the reduction of nitrite to form nitric oxide. In recent years, new classes of redox partner linked CuNiRs have been isolated and characterized by crystallographic techniques. Solution-state biophysical studies have shed light on the complex catalytic mechanisms of these enzymes and implied that protein dynamics may play a role in CuNiR catalysis. To investigate the structural, dynamical, and functional relationship of these CuNiRs, we have used protein reverse engineering and pulsed electron-electron double resonance (PELDOR) spectroscopy to determine their solution-state inter-copper distributions. Data show the multidimensional conformational landscape of this family of enzymes and the role of tethering in catalysis. The importance of combining high-resolution crystallographic techniques and low-resolution solution-state approaches in determining the structures and mechanisms of metalloenzymes is emphasized by our approach.
Keyphrases
- nitric oxide
- high resolution
- single molecule
- solid state
- electron transfer
- solar cells
- nitric oxide synthase
- hydrogen peroxide
- mass spectrometry
- molecular dynamics simulations
- molecular dynamics
- small molecule
- big data
- machine learning
- human immunodeficiency virus
- single cell
- amino acid
- deep learning
- high speed
- hiv testing
- crystal structure
- tandem mass spectrometry
- visible light