000131557 001__ 131557
000131557 005__ 20240319080954.0
000131557 0247_ $$2doi$$a10.1016/j.jinorgbio.2021.111689
000131557 0248_ $$2sideral$$a128235
000131557 037__ $$aART-2022-128235
000131557 041__ $$aeng
000131557 100__ $$aSerra, I.
000131557 245__ $$aImpact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase
000131557 260__ $$c2022
000131557 5203_ $$aChlorite dismutases (Clds) are heme b containing oxidoreductases able to decompose chlorite to chloride and molecular oxygen. This work analyses the impact of the distal, flexible and catalytic arginine on the binding of anionic angulate ligands like nitrite and the substrate chlorite. Dimeric Cld from Cyanothece sp. PCC7425 was used as a model enzyme. We have investigated wild-type CCld having the distal catalytic R127 hydrogen-bonded to glutamine Q74 and variants with R127 (i) being arrested in a salt-bridge with a glutamate (Q74E), (ii) being fully flexible (Q74V) or (iii) substituted by either alanine (R127A) or lysine (R127K). We present the electronic and spectral signatures of the high-spin ferric proteins and the corresponding low-spin nitrite complexes elucidated by UV–visible, circular dichroism and electron paramagnetic resonance spectroscopies. Furthermore, we demonstrate the impact of the dynamics of R127 on the thermal stability of the respective nitrite adducts and present the X-ray crystal structures of the nitrite complexes of wild-type CCld and the variants Q74V, Q74E and R127A. In addition, the molecular dynamics (MD) and the binding modi of nitrite and chlorite to the ferric wild-type enzyme and the mutant proteins and the interaction of the oxoanions with R127 have been analysed by MD simulations. The findings are discussed with respect to the role(s) of R127 in ligand and chlorite binding and substrate degradation.
000131557 536__ $$9info:eu-repo/grantAgreement/EC/H2020/813209/EU/Paramagnetic Species in Catalysis Research. A Unified Approach Towards Heterogeneous, Homogeneous and Enzyme Catalysis/PARACAT$$9This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 813209-PARACAT
000131557 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000131557 590__ $$a3.9$$b2022
000131557 591__ $$aCHEMISTRY, INORGANIC & NUCLEAR$$b8 / 42 = 0.19$$c2022$$dQ1$$eT1
000131557 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b126 / 285 = 0.442$$c2022$$dQ2$$eT2
000131557 592__ $$a0.646$$b2022
000131557 593__ $$aInorganic Chemistry$$c2022$$dQ1
000131557 593__ $$aBiochemistry$$c2022$$dQ2
000131557 594__ $$a7.0$$b2022
000131557 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000131557 700__ $$aSchmidt, D.
000131557 700__ $$aPfanzagl, V.
000131557 700__ $$aMlynek, G.
000131557 700__ $$aHofbauer, S.
000131557 700__ $$aDjinovic-Carugo, K.
000131557 700__ $$aFurtmüller, P. G.
000131557 700__ $$0(orcid)0000-0002-1827-1250$$aGarcía-Rubio, Inés$$uUniversidad de Zaragoza
000131557 700__ $$aVan Doorslaer, S.
000131557 700__ $$aObinger, C.
000131557 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDpto. Física Materia Condensa.$$cÁrea Física Materia Condensada
000131557 773__ $$g227 (2022), 111689 [15 pp.]$$pJ. inorg. biochem.$$tJournal of Inorganic Biochemistry$$x0162-0134
000131557 8564_ $$s3283951$$uhttps://zaguan.unizar.es/record/131557/files/texto_completo.pdf$$yPostprint
000131557 8564_ $$s2373712$$uhttps://zaguan.unizar.es/record/131557/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000131557 909CO $$ooai:zaguan.unizar.es:131557$$particulos$$pdriver
000131557 951__ $$a2024-03-18-13:26:41
000131557 980__ $$aARTICLE