Structural highlights
Function
[NOX_THET8] Can oxidize either NADH or NADPH with a preference for NADH. Can catalyze electron transfer from NADH to various electron acceptors which include, in addition to molecular oxygen, cytochrome c, 2,6 dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue tetrazolium.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structures of the flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) containing isoforms of NADH oxidase from Thermus thermophilus have been determined by isomorphous and molecular replacement and refined to 2.3 A and 1.6 A resolution with R-values of 18.5% and 18.6% respectively. The structure of the homodimeric enzyme consists of a central 4-stranded antiparallel beta-sheet covered by helices, a more flexible domain formed by two helices, and a C-terminal excursion connecting the subunits. The active sites are located in a deep cleft between the subunits. The binding site of the flavin cofactor lacks the common nucleotide binding fold and is different from the FMN binding site found in flavodoxins.
Crystal structure of NADH oxidase from Thermus thermophilus.,Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD Nat Struct Biol. 1995 Dec;2(12):1109-14. PMID:8846223[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD. Crystal structure of NADH oxidase from Thermus thermophilus. Nat Struct Biol. 1995 Dec;2(12):1109-14. PMID:8846223
