000121170 001__ 121170
000121170 005__ 20230519145626.0
000121170 0247_ $$2doi$$a10.3390/antiox10091446
000121170 0248_ $$2sideral$$a131282
000121170 037__ $$aART-2021-131282
000121170 041__ $$aeng
000121170 100__ $$aSánchez-Ruiz, María Isabel
000121170 245__ $$aAgaricales mushroom lignin peroxidase: from structure–function to degradative capabilities
000121170 260__ $$c2021
000121170 5060_ $$aAccess copy available to the general public$$fUnrestricted
000121170 5203_ $$aLignin biodegradation has been extensively studied in white-rot fungi, which largely belong to order Polyporales. Among the enzymes that wood-rotting polypores secrete, lignin peroxidases (LiPs) have been labeled as the most efficient. Here, we characterize a similar enzyme (ApeLiP) from a fungus of the order Agaricales (with ~13,000 described species), the soil-inhabiting mushroom Agrocybe pediades. X-ray crystallography revealed that ApeLiP is structurally related to Polyporales LiPs, with a conserved heme-pocket and a solvent-exposed tryptophan. Its biochemical characterization shows that ApeLiP can oxidize both phenolic and non-phenolic lignin model-compounds, as well as different dyes. Moreover, using stopped-flow rapid spectrophotometry and 2D-NMR, we demonstrate that ApeLiP can also act on real lignin. Characterization of a variant lacking the above tryptophan residue shows that this is the oxidation site for lignin and other high redox-potential substrates, and also plays a role in phenolic substrate oxidation. The reduction potentials of the catalytic-cycle intermediates were estimated by stopped-flow in equilibrium reactions, showing similar activation by H2O2, but a lower potential for the rate-limiting step (compound-II reduction) compared to other LiPs. Unexpectedly, ApeLiP was stable from acidic to basic pH, a relevant feature for application considering its different optima for oxidation of phenolic and nonphenolic compounds.
000121170 536__ $$9info:eu-repo/grantAgreement/ES/CSIC/PIE-202120E019$$9info:eu-repo/grantAgreement/ES/MCIN/FEDER/BIO2017-86559-R
000121170 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000121170 590__ $$a7.675$$b2021
000121170 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b50 / 297 = 0.168$$c2021$$dQ1$$eT1
000121170 591__ $$aFOOD SCIENCE & TECHNOLOGY$$b12 / 144 = 0.083$$c2021$$dQ1$$eT1
000121170 591__ $$aCHEMISTRY, MEDICINAL$$b4 / 63 = 0.063$$c2021$$dQ1$$eT1
000121170 592__ $$a1.008$$b2021
000121170 593__ $$aBiochemistry$$c2021$$dQ1
000121170 593__ $$aPhysiology$$c2021$$dQ1
000121170 593__ $$aMolecular Biology$$c2021$$dQ1
000121170 593__ $$aClinical Biochemistry$$c2021$$dQ1
000121170 594__ $$a6.5$$b2021
000121170 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000121170 700__ $$aAyuso Fernández, Iván
000121170 700__ $$aRencoret, Jorge
000121170 700__ $$0(orcid)0000-0002-5838-0857$$aGonzález Ramírez, Andrés Manuel$$uUniversidad de Zaragoza
000121170 700__ $$aLinde, Dolores
000121170 700__ $$aDavó Siguero, Irene
000121170 700__ $$aRomero, Antonio
000121170 700__ $$aGutiérrez, Ana
000121170 700__ $$aMartínez, Angel T.
000121170 700__ $$aRuiz Dueñas, Francisco Javier
000121170 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000121170 773__ $$g10, 9 (2021), 1446 [23 pp]$$pAntioxidants$$tAntioxidants$$x2076-3921
000121170 8564_ $$s3175809$$uhttps://zaguan.unizar.es/record/121170/files/texto_completo.pdf$$yVersión publicada
000121170 8564_ $$s2834771$$uhttps://zaguan.unizar.es/record/121170/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000121170 909CO $$ooai:zaguan.unizar.es:121170$$particulos$$pdriver
000121170 951__ $$a2023-05-18-16:18:57
000121170 980__ $$aARTICLE