X-ray structure of the iron-peroxide intermediate of superoxide reductase (E114A mutant) from Desulfoarculus baarsii

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.

16 % PEG 4000, 100 MM TRIS/HNO3 PH9.0, 0.2 M CA(NO3)2 AND 25 MG/ML PROTEIN MIXED 1:1, HANGING DROP VAPOUR DIFFUSION, 20C, pH 9.00

STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION

X-RAY STRUCTURE OF WILD-TYPE SUPEROXIDE REDUCTASE FROM DESULFOARCULUS BAARSII

X-RAY STRUCTURE OF E114A MUTANT OF SUPEROXIDE REDUCTASE FROM DESULFOARCULUS BAARSII IN THE NATIVE, REDUCED FORM

ENGINEERED RESIDUE IN CHAIN A, GLU 114 TO ALA ENGINEERED RESIDUE IN CHAIN B, GLU 114 TO ALA ENGINEERED RESIDUE IN CHAIN C, GLU 114 TO ALA ENGINEERED RESIDUE IN CHAIN D, GLU 114 TO ALA

OXIDOREDUCTASE, RAMAN SPECTROSCOPY, SUPEROXIDE REDUCTASE, INTERMEDIATE TRAPPING, MICROSPECTROPHOTOMETRY, DETOXIFICATION, ELECTRON TRANSPORT, IRON, TRANSPORT, REDOX STATES, METAL-BINDING