The role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase

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dc.creatorMozart Silvio Pereira
dc.creatorSimara Semíramis de Araújo
dc.creatorRonaldo Alves Pinto Nagem
dc.creatorJohn P. Richard
dc.creatorTiago Antônio da Silva Brandão
dc.date.accessioned2023-09-29T12:14:58Z
dc.date.accessioned2025-09-09T00:12:03Z
dc.date.available2023-09-29T12:14:58Z
dc.date.issued2022
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Gerais
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.description.sponsorshipINCT – Instituto nacional de ciência e tecnologia (Antigo Instituto do Milênio)
dc.description.sponsorshipOutra Agência
dc.identifier.doihttps://doi.org/10.1016/j.bioorg.2021.105561
dc.identifier.issn1090-2120
dc.identifier.urihttps://hdl.handle.net/1843/59028
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofBioorganic Chemistry
dc.rightsAcesso Restrito
dc.subjectAnálise enzimática
dc.subjectEnzimas - Regulação
dc.subjectCinética de enzimas
dc.subjectMecanismos de reações orgânicas
dc.subjectReações químicas
dc.subjectBioquímica
dc.subject.otherOne-component flavoprotein monooxygenase
dc.subject.otherFlavoenzyme
dc.subject.otherActivation
dc.subject.otherOxidoreductases
dc.subject.otherBiocatalysis
dc.titleThe role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase
dc.typeArtigo de periódico
local.citation.volume119
local.description.resumoSalicylate hydroxylase (NahG) has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol. We report experimental results that show the contribution of individual pieces of the FAD cofactor to the observed enzymatic activity for turnover of the whole cofactor. A comparison of the kinetic parameters and products for the NahG-catalyzed reactions of FMN and riboflavin cofactor fragments reveal that the adenosine monophosphate (AMP) and ribitol phosphate pieces of FAD act to anchor the flavin to the enzyme and to direct the partitioning of the C(4a)-hydroperoxyflavin reaction intermediate towards hydroxylation of salicylate. The addition of AMP or ribitol phosphate pieces to solutions of the truncated flavins results in a partial restoration of the enzymatic activity lost upon truncation of FAD, and the pieces direct the reaction of the C(4a)-hydroperoxyflavin intermediate towards hydroxylation of salicylate.
local.identifier.orcidhttps://orcid.org/0000-0002-1550-8013
local.identifier.orcidhttps://orcid.org/0000-0001-7219-1625
local.identifier.orcidhttps://orcid.org/0000-0002-0440-2387
local.identifier.orcidhttps://orcid.org/0000-0002-7783-3014
local.publisher.countryBrasil
local.publisher.departmentICB - DEPARTAMENTO DE BIOQUÍMICA E IMUNOLOGIA
local.publisher.departmentICX - DEPARTAMENTO DE QUÍMICA
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0045206821009391

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