ArticleJournal of bacteriology2005
Structure and increased thermostability of Rhodococcus sp. naphthalene 1,2-dioxygenase.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 53 citations in OpenAlex.
- Understanding the stability of a plastic-degrading Rieske iron oxidoreductase system.Protein science : a publication of the Protein Society · 2024Article
- Functional and spectroscopic approaches to determining thermal limitations of Rieske oxygenases.Methods in enzymology · 2024Article
- Characterization of a novel aromatic ring-hydroxylating oxygenase, NarA2B2, from thermophilicApplied and environmental microbiology · 2023Article
- Catalytic resilience of multicomponent aromatic ring-hydroxylating dioxygenases in Pseudomonas for degradation of polycyclic aromatic hydrocarbons.World journal of microbiology & biotechnology · 2023Review
- Structural Characterization of the Chlorophyllide a Oxygenase (CAO) Enzyme Through an In Silico Approach.Journal of molecular evolution · 2023Article
- Article
- Article
- Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.Nature communications · 2020Article
- Review
- Spectroscopic Characterisation of the Naphthalene Dioxygenase fromInternational journal of molecular sciences · 2019Article
- The Cell Shape-determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-Carboxypeptidase.The Journal of biological chemistry · 2015Article
- Pleiotropic and epistatic behavior of a ring-hydroxylating oxygenase system in the polycyclic aromatic hydrocarbon metabolic network from Mycobacterium vanbaalenii PYR-1.Journal of bacteriology · 2014Article
- Phylogenetic analysis reveals the surprising diversity of an oxygenase class.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Article
- Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system.Acta crystallographica. Section D, Biological crystallography · 2009Article
- Near-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases.Journal of the American Chemical Society · 2008Article
- Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1.BMC structural biology · 2007Article
- The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1.Biochemical and biophysical research communications · 2007Article
- Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase.Journal of bacteriology · 2006Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Rieske nonheme iron oxygenases form a large class of aromatic ring-hydroxylating dioxygenases found in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth, making them good candidates for use in synthesis of chiral intermediates and bioremediation. Studies of the chemical stability and thermostability of these enzymes thus become important. We report here the structure of free and substrate (indole)-bound forms of naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038. The structure of the Rhodococcus enzyme reveals that, despite a approximately 30% sequence identity between these naphthalene dioxygenases, their overall structures superpose very well with a root mean square deviation of less than 1.6 A. The differences in the active site of the two enzymes are pronounced near the entrance; however, indole binds to the Rhodococcus enzyme in the same orientation as in the Pseudomonas enzyme. Circular dichroism spectroscopy experiments show that the Rhodococcus enzyme has higher thermostability than the naphthalene dioxygenase from Pseudomonas species. The Pseudomonas enzyme has an apparent melting temperature of 55 degrees C while the Rhodococcus enzyme does not completely unfold even at 95 degrees C. Both enzymes, however, show similar unfolding behavior in urea, and the Rhodococcus enzyme is only slightly more tolerant to unfolding by guanidine hydrochloride. Structure analysis suggests that the higher thermostability of the Rhodococcus enzyme may be attributed to a larger buried surface area and extra salt bridge networks between the alpha and beta subunits in the Rhodococcus enzyme.
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