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

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.

2006 ◽  
Vol 362 (1) ◽  
pp. 55-65 ◽  
Author(s):  
Konstantinos Paraskevopoulos ◽  
Svetlana V. Antonyuk ◽  
R. Gary Sawers ◽  
Robert R. Eady ◽  
S. Samar Hasnain

1993 ◽  
Vol 25 (2) ◽  
pp. 121-136 ◽  
Author(s):  
Jonathan P. Hosler ◽  
Shelagh Ferguson-Miller ◽  
Melissa W. Calhoun ◽  
Jeffrey W. Thomas ◽  
John Hill ◽  
...  

2011 ◽  
Vol 16 (2) ◽  
pp. 183-194 ◽  
Author(s):  
Simone Dell’Acqua ◽  
Sofia R. Pauleta ◽  
Isabel Moura ◽  
José J. G. Moura

2015 ◽  
Vol 6 (10) ◽  
pp. 5670-5679 ◽  
Author(s):  
Esther M. Johnston ◽  
Simone Dell'Acqua ◽  
Sofia R. Pauleta ◽  
Isabel Moura ◽  
Edward I. Solomon

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.


2020 ◽  
Author(s):  
Vikram V. Shende ◽  
Yogan Khatri ◽  
Sean A. Newmister ◽  
Jacob N. Sanders ◽  
Petra Lindovska ◽  
...  

This report details the discovery and characterization of a versatile bacterial cytochrome P450, NzeB, which catalyzes the dimerization of diketopiperazines via enzymatic C–H functionalization. This includes the first high-resolution crystal structure of a diketopiperazine dimerase, which along with active site via mutagenesis and quantum mechanical calculations, provides insight into the selectivity and mechanism of these enzymes.


2014 ◽  
Vol 53 (19) ◽  
pp. 10611-10619 ◽  
Author(s):  
Brittany J. Johnson ◽  
Sergey V. Lindeman ◽  
Neal P. Mankad

2020 ◽  
Author(s):  
Vikram V. Shende ◽  
Yogan Khatri ◽  
Sean A. Newmister ◽  
Jacob N. Sanders ◽  
Petra Lindovska ◽  
...  

This report details the discovery and characterization of a versatile bacterial cytochrome P450, NzeB, which catalyzes the dimerization of diketopiperazines via enzymatic C–H functionalization. This includes the first high-resolution crystal structure of a diketopiperazine dimerase, which along with active site via mutagenesis and quantum mechanical calculations, provides insight into the selectivity and mechanism of these enzymes.


2014 ◽  
Vol 5 (12) ◽  
pp. 4774-4784 ◽  
Author(s):  
Charlène Esmieu ◽  
Maylis Orio ◽  
Stéphane Torelli ◽  
Laurent Le Pape ◽  
Jacques Pécaut ◽  
...  

Through a bio-inspired approach of the active site of the metalloenzyme nitrous oxide reductase, we isolated and characterized a dinuclear mixed-valent dicopper complex capable of N2O reduction at room temperature.


Biochimie ◽  
2015 ◽  
Vol 110 ◽  
pp. 73-80 ◽  
Author(s):  
Harish Shukla ◽  
Vikash Kumar ◽  
Amit Kumar Singh ◽  
Neha Singh ◽  
Md. Kashif ◽  
...  

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