Characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase gene cluster
Year: 1999
Type: dissertation
Abstract: Metal chaperone structure and function is an emerging area of research in the field of bioinorganic chemistry.The assembly of the catalytic copper center in nitrous oxide reductase requires the assistance of auxiliary proteins.The isolation, and characterization of these ancillary proteins has not been previously reported.This investigation describes the cloning, recombinant expression, purification, and characterization of NosL from Achromobacter cycloclastes.NosL is an auxiliary protein of the nos (nitrous oxide reductase) gene cluster.Recombinant NosL has a high affinity Cu(I) binding site.Studies to elucidate the function of NosL suggest that it is not the electron-transfer partner to nitrous oxide reductase.In vivo investigations of the phenotype associated with nosL minus strains H t m
Author: Michele A. McGuirl
Language: English
Field: Energy
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W96704072