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2 en the mononuclear iron and Rieske center in naphthalene dioxygenase and in substrate binding and oxy
3 has been implicated in electron transfer in naphthalene dioxygenase and in substrate binding and oxy
4 d identical spectral properties to wild-type naphthalene dioxygenase and was reduced by NADH in the p
6 uncoupler of oxygen consumption in purified naphthalene dioxygenase, did not elicit oxygen uptake by
8 mononuclear nonheme iron proteins, including naphthalene dioxygenase, for which crystal structures ar
10 the catalytic component (ISP(NAR)) of a new naphthalene dioxygenase from Rhodococcus sp. strain NCIM
11 f free and substrate (indole)-bound forms of naphthalene dioxygenase from Rhodococcus sp. strain NCIM
12 reased biodegradation activity and increased naphthalene dioxygenase gene concentrations in the biore
13 Moreover, strain CJ2 hosts the sequence of a naphthalene dioxygenase gene, prevalent in site sediment
18 ty (59 to 78% identity) to the components of naphthalene dioxygenase (NDO) from Pseudomonas strains.
23 ximately 30% sequence identity between these naphthalene dioxygenases, their overall structures super
24 seudomonas fluorescens ATCC 17483 containing naphthalene dioxygenases was associated with moderate ca
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