Intramolecular electron transfer in nitrite reductases.
The copper- and heme-containing nitrite reductases (NiRs) are key enzymes in denitrification. Their subunits contain two distinct redox-active metal centers, an electron-accepting site and a nitrite-reducing site, to carry out the single-electron reduction of nitrite to nitric oxide. Catalytic cycles of both enzyme families employ intramolecular electron transfer that can be rate-determining for their activity. Herein, we report results comparing these two enzyme families in order to resolve the different mechanisms controlling intramolecular electron transfer in these proteins.
Wherland
Scot
S
Department of Chemistry, Washington State University, Pullman, WA 99164-4630, USA.
Farver
Ole
O
Pecht
Israel
I
D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry; D002384:Catalysis; D002627:Chemistry, Physical / Q000379:methods*; D003300:Copper / Q000737:chemistry; D004579:Electron Transport; D004583:Electrons; D006418:Heme / Q000737:chemistry; D008670:Metals / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D009572:Nitrite Reductases / Q000737:chemistry*; D010084:Oxidation-Reduction; D010788:Photosynthesis; D011487:Protein Conformation; D013816:Thermodynamics
D001426:Bacterial Proteins; D008670:Metals; D006418:Heme; D003300:Copper; D009572:Nitrite Reductases