scholarly journals Spectroscopic Definition of the CuZ° Intermediate in Turnover of Nitrous Oxide Reductase and Molecular Insight into the Catalytic Mechanism

2017 ◽  
Vol 139 (12) ◽  
pp. 4462-4476 ◽  
Author(s):  
Esther M. Johnston ◽  
Cíntia Carreira ◽  
Simone Dell’Acqua ◽  
Somdatta Ghosh Dey ◽  
Sofia R. Pauleta ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Catalytic Mechanism ◽  
Nitrous Oxide Reductase ◽  
Definition Of ◽  
Insight Into

Insight into Catalysis of Nitrous Oxide Reductase from High-resolution Structures of Resting and Inhibitor-bound Enzyme from Achromobacter cycloclastes

2006 ◽  
Vol 362 (1) ◽  
pp. 55-65 ◽  
Author(s):  
Konstantinos Paraskevopoulos ◽  
Svetlana V. Antonyuk ◽  
R. Gary Sawers ◽  
Robert R. Eady ◽  
S. Samar Hasnain
Keyword(s):  
Nitrous Oxide ◽  
High Resolution ◽  
Nitrous Oxide Reductase ◽  
Achromobacter Cycloclastes ◽  
Insight Into

scholarly journals Protonation state of the Cu4S2CuZsite in nitrous oxide reductase: redox dependence and insight into reactivity

2015 ◽  
Vol 6 (10) ◽  
pp. 5670-5679 ◽  
Author(s):  
Esther M. Johnston ◽  
Simone Dell'Acqua ◽  
Sofia R. Pauleta ◽  
Isabel Moura ◽  
Edward I. Solomon
Keyword(s):  
Electron Transfer ◽  
Nitrous Oxide ◽  
Redox State ◽  
Nitrous Oxide Reductase ◽  
Protonation State ◽  
Proton Coupled Electron Transfer ◽  
Insight Into

The edge ligand in the Cu4S2CuZform of nitrous oxide reductase is a μ2-thiolate in the 1-hole and a μ2-sulfide in the 2-hole redox state, leading to proton-coupled electron transfer reactivity.

scholarly journals A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase

2021 ◽  
Author(s):  
Lin Zhang ◽  
Eckhard Bill ◽  
Peter M. H. Kroneck ◽  
Oliver Einsle
Keyword(s):  
Nitrous Oxide ◽  
Active Site ◽  
Structural Flexibility ◽  
Nitrous Oxide Reductase ◽  
Metal Site ◽  
And Function ◽  
Insight Into

Variants of all seven histidine ligands of the [4Cu:2S] active site of nitrous oxide reductase mostly result in loss of the metal site. However, a H382A variant retains a [3Cu:2S] cluster that hints towards a structural flexibility also present in the intact site.

Copper–oxygen Dynamics in Tyrosinase

2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Sachiko Yanagisawa ◽  
Minoru Kubo ◽  
Genji Kurisu ◽  
Shinobu Itoh
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Binding ◽  
Active Form ◽  
Copper Ion ◽  
Atomic Resolution ◽  
Oxygen Species ◽  
X Ray ◽  
Oxygen Dynamics ◽  
Insight Into ◽  
Copper Centre

To unveil the activation of dioxygen on the copper centre (Cu<sub>2</sub>O<sub>2</sub>core) of tyrosinase, we performed X-ray crystallograpy with active-form tyrosinase at near atomic resolution. This study provided a novel insight into the catalytic mechanism of the tyrosinase, including the rearrangement of copper-oxygen species as well as the intramolecular migration of copper ion induced by substrate-binding.<br>

The nature of the copper centres in nitrous oxide reductase (Pseudomonas stutzeri)

1991 ◽  
Vol 43 (2-3) ◽  
pp. 181
Author(s):  
Jacqui A. Farrar ◽  
Andrew J. Thomson ◽  
Myles R. Cheesman ◽  
David M. Dooley ◽  
Walter G. Zumft
Keyword(s):  
Nitrous Oxide ◽  
Pseudomonas Stutzeri ◽  
Nitrous Oxide Reductase
Sign in / Sign up

Export Citation Format

Share Document