Cytochrome c nitrite reductase: from structural to physicochemical analysis.
The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-film voltammetry and these are discussed in relation to the essential structural features of the enzyme.
Burlat
B
B
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich NR4 7TJ, UK. b.burlat@uea.ac.uk
Gwyer
J D
JD
Poock
S
S
Clarke
T
T
Cole
J A
JA
Hemmings
A M
AM
Cheesman
M R
MR
Butt
J N
JN
Richardson
D J
DJ
D002942:Circular Dichroism; D045263:Cytochromes a1 / Q000737:chemistry*; D003575:Cytochromes c1 / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D009565:Nitrate Reductases / Q000737:chemistry*; D011487:Protein Conformation
D045263:Cytochromes a1; D003575:Cytochromes c1; D009565:Nitrate Reductases; C054690:nitrate reductase (cytochrome)