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These dioxygenases usually carry out hydroxylation of hydrophobic aromatic compounds and supply substrates with hydroxyl groups for extradiol\/intradiol dioxygenases to cleave rings, and have been extensively studied. Salicylate 5-hydroxylase NagGH is a novel Rieske monooxygenase with high similarity to Rieske dioxygenases, and also shares reductase and ferredoxin similarity with a Rieske dioxygenase naphthalene 1,2-dioxygenase (NagAcAd) in\n            <jats:italic>Ralstonia<\/jats:italic>\n            sp. strain U2.\n          <\/jats:p>","DOI":"10.1128\/aem.01629-20","type":"journal-article","created":{"date-parts":[[2021,1,18]],"date-time":"2021-01-18T12:58:43Z","timestamp":1610974723000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases"],"prefix":"10.1128","volume":"87","author":[{"given":"Yan-Jie","family":"Hou","sequence":"first","affiliation":[{"name":"State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 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